M. Garcia-Chame, P. Wadhwani, J. Pfeifer, U. Schepers, C.M. Niemeyer and C.M. Dominguez. A versatile microfluidic platform for extravasation studies based on DNA origami-cell interactions. Angew. Chem. Int. Ed. 63, e202318805 (2024)

DOI: 10.1002/anie.202318805

A. Hrebonkin, S. Afonin, A. Nikitjuka, O.V. Borysov, G. Leitis, O. Babii, S. Koniev, T. Lorig, S.L. Grage, P. Nick, A.S. Ulrich, A. Jirgensons, I.V. Komarov. Spiropyran-based photoisomerizable α-amino acid for membrane-active peptide modification. Chem. Eur. J. 30, e202400066 (2024)

DOI:10.1002/chem.202400066

S. Mandal, Vijayamohanan.K. Pillai, M.R. Ponraj, Thushara K M, Jebasingh Bhagavathsingh, S.L. Grage, X. Peng, J.W. Kang, D. Liepmann, A.N.M. Kannan, V. Thavasi, Venkatesan Renugopalakrishnan. van der Waals gap modulation of graphene oxide through mono-Boc ethylenediamine anchoring for superior Li-ion batteries. Energy Adv. 3, 1977–1991 (2024)

DOI: 10.1039/d4ya00217b

E. Strandberg, P. Horten, D. Bentz, P. Wadhwani, J. Bürck, A.S.Ulrich. Trp residues near peptide termini enhance the pore-forming activity of cationic amphipathic α-helices. Biophys. Chem. in revision (2024)

Y. Tian, M. Seifermann, L. Bauer, C. Luchena, J.J. Wiedmann, S. Schmidt, A. Geisel, S. Afonin, J. Höpfner, M. Brehm, X. Liu, C. Hopf, A.A. Popova, P.A. Levkin. High-throughput miniaturized synthesis of PROTAC-like molecules. Small 20, e2307215 (2024)

DOI:10.1002/smll.202307215

S. Wörner, P. Rauthe, J. Werner, S. Afonin, A.S. Ulrich, A.N. Unterreiner, H.A. Wagenknecht. Flavin-induced charge separation in transmembrane model peptides. Org. Biomol. Chem. 22, 5930-5935 (2024)

DOI:10.1039/d4ob00932k.

 

H.G. Abernathy, J. Saha, L.K. Kemp, P. Wadhwani, T.D. Clemons, S.E. Morgan, V. Rangachari. De novo amyloid peptides with subtle sequence variations differ in their self-assembly and nanomechanical properties. Soft Matter 19, 5150-5159 (2023)

DOI: 10.1039/d3sm00604b

D. Gauder, A. Bott, J. Gölz, G. Lanza.  Simulation uncertainty determination of single flank rolling tests using monte carlo simulation and skin model shapes for zero defect manufacturing of micro gears. Computers in Industry 146, 103854 (2023)

DOI: 10.1016/j.compind.2023.103854

F. Greil, R. Punampalam, T.H. Walther, S. Heißler, A.S. Ulrich. "Iteratively nafionated water” in its solid phase at room temperature is in fact a mixture of lyophilized biological and non-biological contaminants. J. Mol. Liquids 385, 122351 (2023)

DOI: 10.1016/j.molliq.2023.122351

K. Horbatok, T. Makhnii, V. Kosach, V. Danko, A. Kovalenko, S. Fatiushchenkov, P. Borysko, I. Pishel, O. Babii, A.S. Ulrich, T. Schober, S. Afonin, I.V. Komarov. In vitro and in vivo evaluation of photocontrolled biologically active compounds - potential drug candidates for cancer photopharmacology. J. Vis. Exp. 199, e64902 (2023)

DOI:10.3791/64902

R. Leibe, S. Fritsch-Decker, F. Gussmann, A.M. Wagbo, P. Wadhwani, S. Diabaté, W. Wenzel, A.S. Ulrich, C. Weiss.  Key Role of choline head groups in large unilamellar phospholipid vesicles for the interaction with and rupture by silica nanoparticles. Small 2207593 (2023)

DOI: 10.1002/smll.202207593

C. Li, H. Schopmans, L. Langer, S. Marschner, A. Chandresh, J. Bürck, Y. Tsuchiya, A. Chihaya, W. Wenzel, S. Bräse, M. Kozlowska, L. Heinke. Twisting of porphyrin by assembly in a metal‐organic framework yielding chiral photoconducting films for circularly‐polarized‐light detection. Angew. Chem. Intl. Ed. 62, e202217377 (2023)

DOI: 10.1002/anie.202217377

M. Nishimura, Y. Kawaguchi, K. Kuroki, Y. Nakagawa, T. Masuda, T. Sakai, K. Kawano, H. Hirose, M. Imanishi, T. Takatani-Nakase, S. Afonin, A.S. Ulrich, S. Futaki.  Structural dissection of Epsin‐1 N‐terminal helical peptide: The role of hydrophobic residues in modulating membrane curvature. Chemistry 29, e20230129 (2023)

DOI: 10.1002/chem.202300129
 

E.R. Stockwald, L.M.E. Steger, S. Vollmer, C. Gottselig, S.L. Grage, J. Bürck, S. Afonin, J. Fröbel, A.-S. Blümmel, J. Setzler, W. Wenzel, T.H. Walther, A.S. Ulrich.
Length matters: functional flip of the short TatA transmembrane helix. Biophys. J. 122, 2125-2146 (2023)

DOI: 10.1016/j.bpj.2022.12.016

E. Strandberg, P. Wadhwani, J. Bürck, P. Anders, C. Mink, J. van den Berg, R.A.M. Ciriello, M.N. Melo, M.A.R.B. Castanho, E. Bardají, J.P. Ulmschneider, A.S. Ulrich. Temperature‐Dependent Re‐alignment of the Short Multifunctional Peptide BP100 in Membranes Revealed by Solid‐State NMR Spectroscopy and Molecular Dynamics Simulations. ChemBioChem 24, e202200602 (2022)

DOI: 10.1002/cbic.202200602

K.M. Thushara, M.R. Ponraj, S. Mandal, X. Peng, S.L. Grage, R. Venkatesan, T. Velmurugan, A.M. Kannan, V.K. Pillai, J.W. Kang, J. Bhagavathsingh.
Interlayer, gallery-engineered graphene oxide using selective protection of Mono-Boc-ethylenediamine as anode for sodium ion batteries. J. Energy Storage 73, 109237 (2023)

DOI: 10.1016/j.est.2023.109237
 

B. Zerulla, C. Li, D. Beutel, S. Oßwald, C. Holzer, J. Bürck, S. Bräse, C. Wöll, I. Fernandez-Corbaton, L. Heinke, C. Rockstuhl, M. Krstić. Exploring functional photonic devices made from a chiral metal–organic framework material by a multiscale computational method. Adv. Funct. Mater. 2301093 (2023)

DOI: 10.1002/adfm.202301093

V.E. Diyuk, A.N. Zaderko, L.M. Grishchenko, S. Afonin, R. Mariychuk, M. Kaňuchová, V.V. Lisnyak. Preparation, texture and surface chemistry characterization of nanoporous-activated carbons co-doped with fluorine and chlorine. Applied Nanoscience 12, 2103–2116 (2022)

DOI:10.1007/s13204-022-02459-w

V.E. Diyuk, A.N. Zaderko, L.M. Grishchenko, S. Afonin, R. Mariychuk, O.Y. Boldyrieva, V.A. Skryshevsky, M. Kaňuchová, V.V. Lisnyak. Surface chemistry of fluoroalkylated nanoporous activated carbons: XPS and ¹⁹F NMR study.. Applied Nanoscience 12, 637-650 (2022)

DOI: 10.1007/s13204-021-01717-7

S.L. Grage, S. Afonin, M. Ieronimo, M. Berditsch, P. Wadhwani, A.S. Ulrich. Probing and manipulating the lateral pressure profile in lipid bilayers using membrane-active peptides - A solid-state ¹⁹F NMR study. Intl. J. Mol. Sci. 23, 4544 (2022)

DOI:10.3390/ijms23094544

J.L.S. Lopes, C.C.F. Araujo, R.C. Neves, J. Bürck, S.G. Couto. Structural analysis of the peptides temporin-Ra and temporin-Rb and interactions with model membranes. Eur. Biophys. J. 51, 493–502 (2022)

DOI:10.1007/s00249-022-01615-y

I.V. Komarov, G. Tolstanova, H. Kuznietsova, N. Dziubenko, P.I. Yanchuk, L.Y. Shtanova, S.P. Veselsky, L.V. Garmanchuk, N. Khranovska, O. Gorbach, T. Dovbynchuk, P. Borysko, O. Babii, T. Schober, A.S. Ulrich, S. Afonin. Towards in vivo photomediated delivery of anticancer peptides: Insights from pharmacokinetic and -dynamic data. J. Photochem. Photobiol. B 233, 112479 (2022)

DOI:10.1016/j.jphotobiol.2022.112479

S. Kröll, L. Schneider, P. Wadhwani, K.S. Rabe, C.M. Niemeyer. Orthogonal protein decoration of DNA nanostructures based on SpyCatcher–SpyTag interaction. Chem. Commun. 58, 13471 (2022)

DOI: 10.1039/d2cc05335g

B. Meng, S.L. Grage, O. Babii, M. Takamiya, N. MacKinnon, T. Schober, I. Hutskalov, O. Nassar, S. Afonin, S. Koniev, I.V. Komarov, J.G. Korvink, U. Strähle, A.S. Ulrich. Highly fluorinated peptide probes with enhanced in vivo stability for ¹⁹F‐MRI. Small 18, 2107308 (2022)

DOI:10.1002/smll.202107308

F. Schweigardt, E. Strandberg, P. Wadhwani, J. Reichert, J. Bürck, H.L.P. Cravo, L. Burger, A.S. Ulrich. Membranolytic mechanism of amphiphilic antimicrobial β-stranded [KL]_n peptides. Biomedicines 10, 2071 (2022)
DOI: 10.3390/biomedicines10092071

S. Afonin, S. Koniev, L. Préau, M. Takamiya, A.V. Strizhak, O. Babii, A. Hrebonkin, V.G. Pivovarenko, M. Dathe, F. le Noble, S. Rastegar, U. Strähle, A. S. Ulrich, I. V. Komarov. In vivo behavior of the antibacterial peptide cyclo[RRRWFW], explored using a 3-hydroxychromone-derived fluorescent amino acid. Frontiers Chem. 688446 (2021)

DOI: 10.3389/fchem.2021.688446

O. Babii, S. Afonin, C. Diel, M. Huhn, J. Dommermuth, T. Schober, S. Koniev, A. Hrebonkin, A. Nesterov-Mueller, I.V. Komarov, A.S. Ulrich. Diarylethene-Based Photoswitchable Inhibitors of Serine Proteases. Angew. Chem. 60, 21789-21794.

DOI: 10.1002/anie.202108847

S.L. Grage, A. Culetto, A.S. Ulrich, S. Weinschenk. Membrane-mediated activity of local anesthetics. Mol. Pharmacol. 100, 502-512 (2021)

DOI: 10.1124/molpharm.121.000252

A. B. Kanj, J. Bürck, N. Vankova, C. Li, D. Mutruc, A. Chandresh,S. Hecht, T. Heine, L. Heinke. Chirality remote control in nanoporous materials by circularly polarized light. J. Am. Chem. Soc. 143, 7059−7068 (2021)

DOI: 10.1021/jacs.1c01693

N. Kassem, R. Araya-Secchi, K. Bugge, A. Barclay, H. Steinocher, A. Khondker, Y. Wang, A.J. Lenard, J. Bürck, C. Sahin, A.S. Ulrich, M. Landreh, M.C. Pedersen, M.C. Rheinstädter, P.A. Pedersen, K. Lindorff-Larsen, L. Arleth, B.B. Kragelund. Order and disorder - An integrative structure of the full-length human growth hormone receptor. Sci. Adv. 7, eabh3805 (2021)

DOI: 10.1126/sciadv.abh3805

I. V. Komarov, S. Afonin, O. Babii, T. Schober, A. S. Ulrich, Diarylethenes – molecules with good memory. in: Molecular Photoswitches – Synthesis, Properties and Applications (Editor Z. Pianowski), Wiley-VCH. in press (2021)

V. Kubyshkin, J. Bürck, O. Babii, N. Budisa, A.S. Ulrich. Remarkably high solvatochromism in the circular dichroism spectra of the polyproline-II conformation: limitations or new opportunities? Phys. Chem. Chem. Phys. 23, 26931-26939 (2021)

DOI: 10.1039/d1cp04551b
 

C. Mink, E. Strandberg, P. Wadhwani, M.N. Melo, J. Reichert, I. Wacker, M.A.R.B. Castanho, A.S. Ulrich. Overlapping properties of the short membrane-active peptide BP100 with (i) polycationic TAT and (ii) α-helical magainin family peptides. Front. Cell. Infect. Microbiol. 11, 609542 (2021)

Doi: 10.3389/fcimb.2021.609542

S. Nie, K.-F. Ratzsch, S.L. Grage, J. Keller, A.S. Ulrich, J. Lacayo-Pineda, M. Wilhelm. Correlation between macroscopic elasticity and chain dynamics of natural rubber during vulcanization as determined by a unique rheo-NMR combination. Macromol. 54, 6090-6100 (2021)

DOI: 10.1021/acs.macromol.1c00354

K. R. Sahoo, R. Sharma, S. Bawari, Vivek S., P. K. Rastogi, S.S. Nair, S.L. Grage, T.N. Narayanan. Room-temperature ferromagnetic wide bandgap semiconducting fluorinated graphene-hBN vertical heterostructures. Materials Today Physics 21, 100547 (2021)

DOI: 10.1016/j.mtphys.2021.100547

Y. O. Shaydyuk, N. V. Bashmakova, A. M. Dmytruk, O. D. Kachkovsky, S. Koniev, A. V. Strizhak, I. V. Komarov, K. D. Belfield, M. V. Bondar, O. Babii. Nature of fast relaxation processes and spectroscopy of a membrane-active peptide modified with fluorescent amino acid exhibiting excited state intramolecular proton transfer and efficient stimulated emission. ACS Omega 6, 10119-10128 (2021)

DOI: 10.1021/acsomega.1c00193 

E. Strandberg, P. Wadhwani, A.S. Ulrich. Antibiotic potential and biophysical characterization of amphipathic β-stranded [XZ]_n peptides with alternating cationic and hydrophobic residues. Front. Med. Technol. 3, 622096 (2021)

Doi: 10.3389/fmedt.2021.622096

P. Sun, T. Scharnweber, P. Wadhwani, K.S. Rabe, and C.M. Niemeyer. DNA-directed assembly of a cell-responsive biohybrid interface for cargo release. Small Methods 2001049 (2021)

DOI: 10.1002/smtd.202001049

N. Suryadevara, A. Pausch, E. Moreno-Pineda, A. Mizuno, J. Bürck, A. Baksi, T. Hochdörffer, I. Šalitroš, A.S. Ulrich, M.M. Kappes, V. Schünemann,  W. Klopper, M. Ruben. Chiral Resolution of Spin-Crossover Active Iron(II) [2x2] Grid Complexes. Chemistry Eur. J. 27, 15172-15180 (2021)

DOI: 10.1002/chem.202101432

P. Wadhwani, S. Sekaran, E. Strandberg, J. Bürck, A. Chugh, A.S. Ulrich. Membrane interactions of latarcins: antimicrobial peptides from spider venom. Int. J. Mol. Sci. 22, 10156 (2021)

DOI: 10.3390/ijms221810156.

Z. Wang, H. Cui, M. Liu, S.L. Grage, M. Hoffmann, E. Sedghamiz, M. Wilhelm, W. Wenzel, P.A. Levkin. Tough, transparent, 3D printable and self-healing polyethylene glycol-gel (PEGgel). Adv. Materials (2021) in press

S. Afonin, O. Babii, A. Reuter, V. Middel, M. Takamiya, U. Strähle, I.V. Komarov, A.S. Ulrich. Light-controllable dithienylethene-modified cyclic peptides: photoswitching the in vivo toxicity in zebrafish embryos. Beilstein J. Org. Chem. 16, 38-49 (2020)

DOI: 10.3762/bjoc.16.6

O. Babii, S. Afonin, T. Schober, L. V. Garmanchuk, L. I. Ostapchenko, V. Yurchenko, S. Zozulya, O. Tarasov, I. Pishel, A. S. Ulrich, I. V. Komarov. Peptide drugs for photopharmacology: how much of a safety advantage can be gained by photocontrol? Future Drug Discov. 2, FDD28 (2020)

DOI: 10.4155/fdd-2019-0033

M. Brehm, S. Heissler, S. Afonin, P.A. Levkin. Nanomolar synthesis in droplet microarrays with UV-triggered on-chip cell screening. Small 1905971 (2020)

DOI: 10.1002/smll.201905971

M. Drouin, P. Wadhwani, S.L. Grage, J. Bürck, J. Reichert, S. Tremblay, M.S. Mayer, C. Diel, A. Staub, J.-F. Paquin, A.S. Ulrich. Monofluoroalkene-isostere as a ¹⁹F-NMR label for the peptide backbone: synthesis and evaluation in membrane-bound PGLa and (KIGAKI)₃. Chemistry Eur. J. 26, 1511-1517 (2020)

DOI: 10.1002/chem.201905054

S. L. Grage, S. Afonin, A. S. Ulrich. ¹⁹F NMR in biomembranes. In "Solid state NMR: Applications in Biomembrane Structure" (Ed. F. Separovic and M. A. Sani), IOP Publishing, pages 6.1-6.43 (2020)

W.-H. Hsu, T. Masuda, S. Afonin, T. Sakai, J.V.V. Arafiles, K. Kawano, H. Hirose, M. Imanishi, A.S.Ulrich, S. Futaki.  Enhancing the activity of membrane remodeling epsin-peptide by trimerization. Bioorg. Med. Chem. Lett. 30, 127190 (2020)

DOI: 10.1016/j.bmcl.2020.127190

M. Serulla, G. Ichim, F. Stojceski, G. Grasso, S. Afonin, M. Heulot, T. Schober, R. Roth, C. Godefroy, P.-E. Milhiet, K. Das, A. J. García-Sáez, A. Danani, C. Widmann. TAT-RasGAP317-326 kills cells by targeting inner-leaflet–enriched phospholipids. Proc. Natl. Acad. Sci. USA 117, 31871-31881 (2020)

DOI: 10.1073/pnas.2014108117

R. Sharma, T. C. Asmara, K. Rani Sahoo, S. L. Grage, R. Zhang, J. Sun, S. Das, A. S. Ulrich, A. Rusydi, S. Aryasomayajula, R. Paulmurugan, D. Liepmann, D. Sakthi Kumar, P. Somasundaran, V. Renugopalakrishnan, T. N. Narayanan. Structural and Electronic Transport Properties of Fluorographene Directly Grown on Silicates for Possible Biosensor Applications. ACS Appl. Nano Mater. 3, 5399–5409 (2020)

DOI: 10.1021/acsanm.0c00768

L. M. E. Steger, A. Kohlmeyer, P. Wadhwani, J. Bürck, E. Strandberg, J. Reichert, S. L. Grage, S. Afonin, M. Kempfer, A. C. Görner, J. Koch, T. H. Walther, A. S. Ulrich. Structural and functional characterization of the pore forming domain of pinholin S₂₁68. Proc.  Natl. Acad. Sci. 117, 29637-29646 (2020)

DOI: 10.1073/pnas.2007979117

E. Strandberg, F. Schweigardt, P. Wadhwani, J. Bürck, J. Reichert, H. L. P. Cravo, L. Burger, A. S. Ulrich. Phosphate‑dependent aggregation of [KL]n peptides affects their membranolytic activity. Sci. Rep. 10, 12300 (2020)

DOI: 10.1038/s41598-020-69162-0

E. Strandberg, D. Bentz, P. Wadhwani, A. S. Ulrich. Chiral supramolecular architecture of stable transmembrane pores formed by an α-helical antibiotic peptide in the presence of lyso-lipids. Sci. Rep. 10, 4710 (2020)

DOI: 10.1038/s41598-020-61526-w

E. Strandberg, D. Bentz, P. Wadhwani, J. Bürck, A. S. Ulrich. Terminal charges modulate the pore forming activity of cationic amphipathic helices. Biochim. Biophys. Acta 1862, 183243 (2020)

DOI: 10.1016/j.bbamem.2020.183243

A. V. Strizhak, O. Babii, S. Afonin, I. Bakanovich, T. Pantelejevs, W. Xu, E. Fowler, R. Eapen, K. Sharma, M. O. Platonov, V. V. Hurmach, L. Itzhaki, M. Hyvönen, A. S. Ulrich, D. R. Spring, I. V. Komarov. Diarylethene moiety as an enthalpy-entropy switch: photoisomerizable stapled peptides for modulating p53/MDM2 interaction. Org. Biomol. Chem. 18, 5359-5369 (2020)

DOI: 10.1039/d0ob00831a

S. Wörner, F. Rönicke, A.S. Ulrich, H.A. Wagenknecht. 4-Aminophthalimide as small and environment-sensitive fluorescent amino acid to probe transmembrane peptides. ChemBioChem 21, 618-622 (2020)

DOI: 10.1002/cbic.201900520

Z. You, M. Behl, S.L. Grage, J. Bürck, Q. Zhao, A.S. Ulrich, A. Lendlein. Shape-memory effect by sequential coupling of functions over different length scales in an architectured hydrogel. Biomacromolecules 21, 680-687 (2020)

DOI: 10.1021/acs.biomac.9b01390

M. Berditsch, S. Afonin, J. Reuster, H. Lux, K. Schkolin, O. Babii, D.S. Radchenko, I. Abdullah, N. William, V. Middel, U. Strähle, A. Nelson, K. Valko, A.S. Ulrich. Supreme activity of gramicidin S against resistant, persistent and biofilm cells of  staphylococci and enterococci. Sci. Rep. 9, 17983 (2019)

DOI: 10.1038/s41598-019-54212-z

B. Casciaro, Q. Lin, Q., S. Afonin,  M.R. Loffredo,  V. de Turris,  V. Middel,  A.S. Ulrich,  Y.P. Di,  L.M. Mangoni. Inhibition of Pseudomonas aeruginosa biofilm formation and expression of virulence genes by selective epimerization in the peptide Esculentin-1a(1-21)NH2. FEBS Journal 286, 3874-3891 (2019)

DOI: 10.1111/febs.14940

I.‐L. Hsiao, S. Fritsch‐Decker, A. Leidner, M. Al‐Rawi, V. Hug, S. Diabaté, S.L. Grage, M. Meffert, T. Stoeger, D. Gerthsen, A.S. Ulrich, C.M. Niemeyer, C. Weiss. Biocompatibility of amine‐functionalized silica nanoparticles: The role of surface coverage. Small 1805400 (2019)

DOI: 10.1002/smll.201805400

A.B. Kanj, J. Bürck, S. Grosjean, S. Bräse, L. Heinke. Switching the enantioselectivity of nanoporous host materials by light. Chem. Commun. 55, 8776 (2019)

DOI: 10.1039/C9CC02849H

I.V. Komarov, S. Afonin, A.S. Ulrich. ¹⁹F-labelled amino acids for NMR structure analysis of membrane-bound peptides, in "Fluorine in life sciences: pharmaceuticals, medicinal diagnostics, and agrochemicals" (Eds. G. Haufe and F. Léroux)

DOI: 10.1016/B978-0-12-812733-9.00010-6

V. Kubyshkin, S.L. Grage, A. S. Ulrich, N. Budisa. Bilayer thickness determines the alignment of model
polyproline helices in lipid membranes. Phys. Chem. Chem. Phys. 21, 22396-22408 (2019)

DOI: 10.1039/c9cp02996f

P.S. Kumagai, V.K. Sousa, M. Donato, R. Itri, L.M. Beltramini, A.P.U. Araujo, J. Bürck, B.A. Wallace, J.L.S. Lopes. Unveiling the binding and orientation of the antimicrobial peptide Plantaricin 149 in zwitterionic and negatively charged membranes. Eur. Biophys. J. 48, 621–633 (2019)

DOI: 10.1007/s00249-019-01387-y

P.-A. Paquet-Côté, M. Fillion, M.-È. Provencher, F. Otis, J. Dionne, S. Cardinal, B. Collignon, J. Bürck, P. Lagüe, A.S. Ulrich, M. Auger, N. Voyer. Crown ether modified peptide interactions with model membranes. Supramol. Chem. 31, 159-171 (2019)

DOI: 10.1080/10610278.2019.1574349

A. Raasakka, S. Ruskamo, J. Kowal, H. Han, A. Baumann, M. Myllykoski, A. Fasano, R. Rossano, P. Riccio, J. Bürck, A.S. Ulrich, H. Stahlberg, P. Kursula. Molecular structure and function of myelin protein P0 in membrane stacking. Sci. Rep. 9:642 (2019)

DOI: 10.1038/s41598-018-37009-4

V. Schneider, P. Wadhwani, J. Reichert, J. Bürck, M. Elstner, A.S. Ulrich, T. Kubar. Tetrameric charge-zipper assembly of the TisB peptide in membranes - computer simulation and experiment. J. Phys. Chem. B 123, 1770-1779 (2019)

DOI: 10.1021/acs.jpcb.8b12087

T. Schober, I. Wehl, S. Afonin, O. Babii, A. Iampolska, U. Schepers, I.V. Komarov, A.S. Ulrich. Controlling the uptake of diarylethene‐based cell‐penetrating peptides into cells using light. ChemPhotoChem 3, 384-391 (2019)

DOI: 10.1002/cptc.201900019

C. Schweigert, O. Babii, S. Afonin, T. Schober, N.C. Michenfelder, J. Leier, I.V. Komarov, A.S. Ulrich, and A.N. Unterreiner. Real-time observation of dithienylethene-based photoswitches in a cyclic peptide environment. ChemPhotoChem 3, 403-410 (2019)

DOI: 10.1002/cptc.201900005

E. Strandberg, A.S. Ulrich. Flow charts for the systematic solid-state ¹⁹F/²H-NMR structure analysis of membrane-bound peptides. Ann. Rep. NMR Spect. 99, 79 (2019)

DOI: 0.1016/bs.arnmr.2019.08.002

M. Tabasinezhad, F. Mahboudi, W. Wenzel, H. Rahimi, T. Walther, C. Blattner, E. Omidinia. The transient production of anti-TNF-α antibody Adalimumab and a comparison of its characterization to the biosimilar Cinorra. Prot. Expr. Purif. 155, 59-65 (2019)

DOI: 10.1016/j.pep.2018.11.006

A.N. Zaderko, R.Y. Shvets, I.I. Grygorchak, S.  Afonin, V.E. Diyuk, R.T. Mariychuk, O.Y. Boldyrieva, M. Kaňuchová, V.V. Lisnyak. Fluoroalkylated nanoporous carbons: Testing as a supercapacitor electrode. Appl. Surf. Sci. 470, 882-892 (2019)

DOI: 10.1016/j.apsusc.2018.11.141

V. Kubyshkin, S.L. Grage, J. Bürck, A.S. Ulrich, N. Budisa. Transmembrane polyproline helix. J. Phys. Chem. Lett. 9, 2170–2174 (2018)

DOI :10.1021/acs.jpclett.8b00829

O. Babii, S. Afonin, A.Y. Ishchenko, T. Schober, A.O. Negelia, G.M. Tolstanova, L.V. Garmanchuk, L.I. Ostapchenko, I.V. Komarov, A.S. Ulrich. Structure-activity relationships of photoswitchable diarylethene-based β-hairpin peptides as membranolytic antimicrobial and anticancer agents. J. Med. Chem. 61, 10793-10813 (2018)

DOI: 10.1021/acs.jmedchem.8b01428

S. Reißer, E. Strandberg, T. Steinbrecher, M. Elstner, A.S. Ulrich. Best of two worlds? How MD simulations of amphiphilic helical peptides in membranes can complement data from oriented solid-state NMR. J. Chem. Theory Comput. 14, 6002-6014 (2018)

DOI: 10.1021/acs.jctc.8b00283

S.L. Grage, S. Kara, A. Bordessa, V. Doan, F. Rizzolo, M. Putzu, T. Kubař, A.M. Papini, G. Chaume, T. Brigaud, S. Afonin, A.S. Ulrich. Orthogonal ¹⁹F-labeling for solid-state NMR spectroscopy reveals the conformation and orientation of short peptaibols in membranes. Chemistry Eur. J. 24, 4328–4335 (2018)

DOI: 10.1002/chem.201704307

I.V. Komarov, S. Afonin, O. Babii, T. Schober, A.S. Ulrich. Efficiently photocontrollable or not? Biological activity of photoisomerizable diarylethenes. Chemistry Eur. J. 24, 11245-11254 (2018)

DOI: 10.1002/chem.201801205

H. Zamora-Carreras, B. Maestro, E. Strandberg, A.S. Ulrich, J.M. Sanz, M.Á. Jiménez. Roles of amphipathicity and hydrophobicity in the micelle-driven structural switch of a 14-mer peptide core from a choline-binding repeat. Chemistry Eur. J. 24, 5825–5839 (2018)

DOI: 10.1002/chem.201704802

E. Strandberg, A. Grau-Campistany, P. Wadhwani, J. Bürck, F. Rabanal, A.S. Ulrich. Helix fraying and lipid-dependent structure of a short amphipathic membrane-bound peptide revealed by solid-state NMR. J. Phys. Chem. B 122, 6236-6250 (2018)

DOI: 10.1021/acs.jpcb.8b02661

P. Ridone, S.L. Grage, A. Patkunarajah, A.R. Battle, A.S. Ulrich, B. Martinac. "Force-from-lipids" gating of mechanosensitive channels modulated by PUFAs. J. Mech. Beh. Biomed. Mat. 79, 158-167 (2018)

DOI: 10.1016/j.jmbbm.2017.12.026

M.-C. Gagnon, E. Strandberg, A.S. Ulrich, J.-F. Paquin, M. Auger. New insights into the influence of monofluorination on dimyristoylphosphatidylcholine membrane properties: A solid-state NMR study. Biochim. Biophys. Acta -  Biomembranes 1860, 654-663 (2018)

DOI: 10.1016/j.bbamem.2017.12.002

A.V. Strizhak, K. Sharma, O. Babii, S. Afonin, A.S. Ulrich, I.V. Komarov, D.R. Spring. Highly reactive bis-cyclooctyne-modified diarylethene for SPAAC-mediated cross-linking. Org. Biomol. Chem. 16, 8559–8564 (2018)

DOI: 10.1039/c8ob02428f

O.M. Michurin, K. Tolmachova, S. Afonin, O. Babii, S.L. Grage, A.S. Ulrich, I.V. Komarov, D.S. Radchenko.  Conformationally constrained mono-fluorinated arginine as a cationic label for solid-state 19F NMR analysis of membrane-bound peptides. Eur. J. Org. Chem. 2018, 3826–3833 (2018)

DOI: 10.1002/ejoc.201800473

J. Bürck, O. Aras, L. Bertinetti, C.A. Ilhan, M.A. Ermeydan, R. Schneider, A.S. Ulrich, M. Kazanci. Observation of triple helix motif on electrospun collagen nanofibers and its effect on the physical and structural properties. J. Mol. Struct. 1151, 73-80 (2018)

DOI: 10.1016/j.molstruc.2017.09.030

S. Reißer, S. Prock, H. Heinzmann, A.S. Ulrich. Protein ORIGAMI: A program for the creation of 3D paper models of folded peptides. Biochem. Mol. Biol. Education 46, 403–409 (2018)

DOI: 10.1002/bmb.21132

S. Afonin, V. Kubyshkin, P.K. Mykhailiuk, I.V. Komarov, A.S. Ulrich. Conformational plasticity of the cell-penetrating peptide SAP as revealed by solid-state 19F-NMR and circular dichroism spectroscopies.  J. Phys. Chem. B 121, 6479-6491 (2017)

DOI: 10.1021/acs.jpcb.7b02852

O. Babii, S. Afonin, T. Schober, I.V. Komarov, A.S. Ulrich. Flexibility vs rigidity of amphipathic peptide conjugates when interacting with lipid bilayers. Biochim. Biophys. Acta 1859, 2505-2515 (2017)

DOI:10.1016/j.bbamem.2017.09.021

M. Berditsch, M. Trapp, S. Afonin, C. Weber, J. Misiewicz, J. Turkson, A.S. Ulrich. Antimicrobial peptide gramicidin S is accumulated in granules of producer cells for storage of bacterial phosphagens. Sci. Rep. 7, 44324 (2017)

DOI: 10.1038/srep44324

K. Eggenberger, P. Sanyal, S. Hundt, P. Wadhwani, A.S. Ulrich, P. Nick. Challenge integrity: The cell-penetrating peptide BP100 interferes with the auxin-actin oscillator. Plant Cell Physiol. 58, 71-85 (2017)

DOI: 10.1093/pcp/pcw161

M.-C. Gagnon, E. Strandberg, A. Grau-Campistany, P. Wadhwani, J. Reichert, J. Bürck, F. Rabanal, M. Auger, J.-F. Paquin, A.S. Ulrich. Influence of length and charge on the activity of α-helical amphipathic antimicrobial peptides. Biochem. 56, 1680−1695 (2017) DOI: 10.1021/acs.biochem.6b01071

S.L. Grage, M.-A. Sani, O. Cheneval, S. Troeira Henriques, C. Schalck, R. Heinzmann, J.S. Mylne, P.K. Mykhailiuk, S. Afonin, I.V. Komarov, F. Separovic, D.J. Craik, A.S. Ulrich. Orientation and location of the cyclotide kalata B1 in phospholipid bilayers revealed by solid-state NMR. Biophys. J. 112, 630-642 (2017)

DOI: 10.1016/j.bpj.2016.12.040

S. Kara, S. Afonin, O. Babii, A.N. Tkachenko, I.V. Komarov, A.S. Ulrich. Diphytanoyl lipids as model systems for studying membrane-active peptides. Biochim. Biophys. Acta 1859, 1828-1837 (2017)

DOI: 10.1016/j.bbamem.2017.06.003

M.J. Klein, S. Schmidt, P. Wadhwani, J. Bürck, J.Reichert, S. Afonin, M. Berditsch, T. Schober, R. Brock, M. Kansy, A.S. Ulrich. Lactam-stapled cell-penetrating peptides: Cell uptake and membrane binding properties. J. Med. Chem. 60, 8071-8082 (2017)

DOI: 10.1021/acs.jmedchem.7b00813

L. Li, M. Schmitt, A. Matzke-Ogi, P. Wadhwani, V. Orian-Rousseau, P.A. Levkin. CD44v6-peptide functionalized nanoparticles selectively bind to metastatic cancer cells. Adv. Sci. 4, 1600202 (2017)

DOI: 10.1002/advs.201600202

P. Mühlhäuser, P. Wadhwani, E. Strandberg, J. Bürck, A.S. Ulrich. Structure analysis of the membrane-bound DCD-derived peptide SSL-25 from human sweat. Biochim. Biophys. Acta 1859, 2308-2318 (2017)

DOI: 10.1016/j.bbamem.2017.09.004

T. Murayama, T. Masuda, S. Afonin, K. Kawano, T. Takatani-Nakase, H. Ida, Y. Takahashi, T. Fukuma, A.S. Ulrich, S. Futaki. Loosening of lipid packing promotes oligoarginine entry into cells. Angew. Chem. Int. Ed. 56, 7644-7647 (2017)

DOI: 10.1002/anie.201703578

C. Priem, A. Wuttke, M. Berditsch, A.S. Ulrich, A. Geyer. Scaling the amphiphilic character and antimicrobial activity of Gramicidin S by dihydroxylation or ketal formation. J. Org. Chem. in press (2017)

DOI: 10.1021/acs.joc.7b02177

M. Putzu, S. Kara, S. Afonin, S.L. Grage, A. Bordessa, G. Chaume, T. Brigaud , A.S. Ulrich, T. Kubař. Structural behavior of the peptaibol Harzianin HK VI in a DMPC bilayer: Insights from MD simulations. Biophys. J. 112, 2602-2614 (2017)

DOI: 10.1016/j.bpj.2017.05.019

S. Reißer, D. Poger, M. Stroet, A.E. Mark. Real Cost of Speed: The Effect of a Time-Saving Multiple-Time-Stepping Algorithm on the Accuracy of Molecular Dynamics Simulations. J. Chem. Theory Comput. 13, 2367-2372 (2017)

DOI: 10.1021/acs.jctc.7b00178

A. Raasakka, S. Ruskamo, J. Kowal, R. Barker, A. Baumann, A. Martel, J. Tuusa, M. Myllykoski, J. Bürck, A.S. Ulrich, H. Stahlberg, P. Kursula. Membrane association landscape of myelin basic protein portrays formation of the myelin major dense line. Sci. Rep. 7: 4974 (2017)

DOI:10.1038/s41598-017-05364-3

E. Strandberg, A.S. Ulrich. Solid-state 19F-NMR analysis of peptides in oriented biomembranes. In: Modern Magnetic Resonance, pages 1-18. (Springer International Publishing, 2017, ed. Graham A. Webb)

DOI: 10.1007/978-3-319-28275-6_88-1

E. Strandberg, A.S. Ulrich (2017). Solid-state NMR for studying peptide structures and peptide-lipid interactions in membranes. In:  Modern Magnetic Resonance, pages 1-13. (Springer International Publishing, 2017, ed. Graham A. Webb)

DOI: 10.1007/978-3-319-28275-6_114-1

H. Turgut, A.C. Schmidt, P. Wadhwani, A. Welle, R. Müller, G. Delaittre.  The para-fluoro-thiol ligation in water. Polymer Chem. 8, 1288-1293 (2017)

DOI: 10.1039/C6PY02108E

A. Turshatov, D. Busko, N. Kiseleva, S.L. Grage, I.A. Howard, B.S. Richards. Room-temperature high-efficiency solid-state triplet-triplet annihilation up-conversion in amorphous poly(olefin sulfone)s. ACS Appl. Mat. Interf. 9, 8280-8286 (2017)

DOI:10.1021/acsami.6b12625

J. Zerweck, E. Strandberg, O. Kukharenko, J. Reichert, J. Bürck, P. Wadhwani, A.S. Ulrich. Molecular mechanism of synergy between the antimicrobial peptides PGLa and magainin 2. Sci. Rep. 7, 13153 (2017)

DOI: 10.1038/s41598-017-12599-7

P. Wadhwani, N. Heidenreich, B. Podeyn, J. Bürck, A.S. Ulrich. Antibiotic gold: tethering of antimicrobial peptides to gold nanoparticles maintains conformational flexibility of peptides and improves trypsin susceptibility. Biomater. Sci. 5, 817-827 (2017)

DOI: 10.1039/C7BM00069C

R. Wallbrecher, T. Ackels, R.A. Olea, M.J. Klein, L. Caillon, J. Schiller, P.H. Bovée-Geurts, T.H. van Kuppevelt, A.S. Ulrich, M. Spehr, M.J.W. Adjobo-Hermans, R. Brock. Membrane permeation of arginine-rich cell-penetrating peptides independent of transmembrane potential as a function of lipid composition and membrane fluidity. J. Contr. Release 256, 68-78 (2017)

DOI: 10.1016/j.jconrel.2017.04.013

O. Babii, S. Afonin, L.V. Garmanchuk, V.V. Nikulina, T.V. Nikolaienko, O.V. Storozhuk, D.V. Shelest, O.I. Dasyukevich, O.I., L.I. Ostapchenko, V. Iurchenko, S. Zozulya, A.S. Ulrich, I.V. Komarov. Direct photocontrol of peptidomimetics: an alternative to oxygen-dependent photodynamic cancer therapy. Angewandte Chemie - International Edition 55, 5493-5496 (2016)

DOI: 10.1002/anie.201600506

G. Batoni, M. Casu, A. Giuliani, V. Luca, G. Maisetta, M.L. Mangoni, G. Manzo, M. Pintus, G. Pirri, A.C. Rinaldi, M.A. Scorciapino, I. Serra, A.S. Ulrich, P. Wadhwani. Rational modification of a dendrimeric peptide with antimicrobial activity: Consequences on membrane-binding and biological properties. Amino Acids 48, 887-900 (2016)

DOI: 10.1007/s00726-015-2136-5

M. Berditsch, H. Lux, O. Babii, S. Afonin, A.S. Ulrich. Therapeutic potential of gramicidin S in the treatment of root canal infections. Pharmaceuticals 9, 56 (2016)

DOI: 10.3390/ph9030056

J. Bürck, P. Wadhwani, S. Fanghänel, A.S. Ulrich. Oriented Circular Dichroism: A Method to Characterize Membrane-Active Peptides in Oriented Lipid Bilayers. Acc. Chem. Res. 49, 184-192 (2016)

DOI: 10.1021/acs.accounts.5b00346

N. Gao, P. Wadhwani, P. Mühlhäuser, Q. Liu, M. Riemann, A.S. Ulrich, P. Nick. An antifungal protein from Ginkgo biloba binds actin and can trigger cell death. Protoplasma 253, 1159-1174 (2016)

DOI: 10.1007/s00709-015-0876-4

S.L. Grage, S. Afonin, S. Kara, G. Buth, A.S. Ulrich. Membrane Thinning and Thickening Induced by Membrane-Active Amphipathic Peptides. Frontiers in Cell and Developmental Biology 4, 65 (2016)

DOI: 10.3389/fcell.2016.00065

A. Grau-Campistany, E. Strandberg, P. Wadhwani, F. Rabanal, A.S. Ulrich. Extending the hydrophobic mismatch concept to amphiphilic membraneolytic peptides. J. Phys. Chem. Lett. 7, 1116-1120 (2016)

DOI: 10.1021/acs.jpclett.6b00136

S.O. Kokhan, A.V. Tymtsunik, S.L. Grage, S. Afonin S., O. Babii, M. Berditsch, A.V. Strizhak, D. Bandak, M.O. Platonov, I.V. Komarov, A.S. Ulrich, P.K. Mykhailiuk. Design, synthesis, and application of an optimized monofluorinated aliphatic label for peptide studies by solid-state 19F NMR spectroscopy. Angewandte Chemie - Intl. Ed. 55, 14788-14792 (2016) DOI: 10.1002/anie.201608116

O. M. Michurin, S. Afonin, M. Berditsch, C.G. Daniliuc, A.S. Ulrich, I.V. Komarov, D.S. Radchenko. Delivering structural information on the polar face of membrane-active peptides: 19F-NMR labels with a cationic side chain. Angewandte Chemie - International Edition 55, 14595-14599 (2016)

DOI: 10.1002/anie.201607161

D.S. Radchenko, S. Kattge, S. Kara, A.S. Ulrich A.S., S. Afonin. Does a methionine-to-norleucine substitution in PGLa influence peptide-membrane interactions? Biochim. Biophys. Acta 1858, 2019-27 (2016)

DOI: 10.1016/j.bbamem.2016.06.002

E. Strandberg, D. Horn, S. Reißer, J. Zerweck, P. Wadhwani, A.S. Ulrich. 2H-NMR and MD simulations reveal membrane-bound conformation of magainin 2 and its synergy with PGLa. Biophys. J. 111, 2149-2161 (2016)

DOI: 10.1016/j.bpj.2016.10.012

C.M. Thiele, A.S. Ulrich. Light flips a membrane-embedded helix. Science 352, 520 (2016)

DOI: 10.1126/science.aaf6191

H. Zamora-Carreras, E. Strandberg, P. Mühlhäuser, J. Bürck, P. Wadhwani, M. Ángeles Jiménez, M. Bruix, A.S. Ulrich. Alanine scan and 2H-NMR analysis of the membrane-active peptide BP100 points to a distinct carpet mechanism of action. Biochim. Biophys. Acta 1858, 1328-1338 (2016)

DOI: 10.1016/j.bbamem.2016.03.014

J. Zerweck, E. Strandberg, J. Bürck, J. Reichert, P. Wadhwani, O. Kukharenko, A.S. Ulrich. Homo- and heteromeric interaction strengths of the synergistic antimicrobial peptides PGLa and magainin 2 in membranes. Eur. Biophys. J. 46, 535–547 (2016)

DOI: 10.1007/s00249-016-1120-7

N. Zydziak, W. Konrad, F. Feist, S. Afonin, S. Weidner, C. Barner-Kowollik. Coding and decoding libraries of sequence-defined functional copolymers synthesized via photoligation. Nature Comm. 7, 13672 (2016)

DOI: 10.1038/ncomms13672

A. Grau-Campistany, E. Strandberg, P. Wadhwani, J. Reichert, J. Bürck, F. Rabanal and A. S. Ulrich. Hydrophobic mismatch demonstrated for membranolytic peptides, and their use as molecular rulers to measure bilayer thickness in native cells. Scientific Reports 5, 9388 (2015)
DOI:10.1038/srep09388

T. Asakura, T. Ohata, S. Kametani, K. Okushita, K. Yazawa, Y. Nishiyama, K. Nishimura, A. Aoki, F. Sizuki, H. Kaji, A. S. Ulrich, M. P. Williamson. Intermolecular packing in B. mori silk fibroin: Multinuclear NMR study of the model peptide (Ala-Gly)15 defines a heterogeneous antiparallel antipolar mode of assembly in the silk II form. Macromolecules 48, 28-36 (2015)
DOI: 10.1021/ma502191g

D. Bandak, O. Babii, R. Vasiuta, I. V. Komarov, P. K. Mykhailiuk. Design and synthesis of novel 19F-amino acid: A promising 19F NMR label for peptide studies. Org. Lett. 17, 226-229 (2015)
DOI:10.1021/ol503300m

M. Berditsch, S. Afonin, A. Steineker, N. Orel, I. Jakovkin, C. Weber and A. S. Ulrich. Fermentation and cost-effective 13C/15N labeling of the nonribosomal peptide gramicidin S for nuclear magnetic resonance structure analysis. Appl. Environ. Microbiol. 81, 3593-3603 (2015)
DOI:10.1128/AEM.00229-15

M. Berditsch, T. Jäger, N. Strempel, T. Schwartz, J. Overhage and A. S. Ulrich. Synergistic effect of membrane active peptides polymyxin B and gramicidin S on multidrug resistant strains and biofilms of Pseudomonas aeruginosa. Antimicrobial Agents and Chemotherapy 59, 5288-5296 (2015)
DOI:10.1128/AAC.00682-15

D. S. Blokhin, A. V. Filippov, O. N. Antzutkin, S. Afonin and V. V. Klochkov. Spatial structures of PAP(262 270) and PAP(274 284), two selected fragments of PAP(248 286), an enhancer of HIV infectivity. Appl. Magn. Reson. 46, 757-769 (2015)
DOI:10.1007/s00723-015-0669-0

J. Bürck, S. Roth, D. Windisch, P. Wadhwani, D. Moss and A. S. Ulrich. UV-CD12: synchrotron radiation circular dichroism beamline at ANKA. Journal of Synchrotron Radiation 22, 844-852 (2015)
DOI:10.1107/S1600577515004476

M. Cakici, Z.-G. Gu, M. Nieger, J. Bürck, L. Heinke and S. Bräse. Planar-chiral building blocks for metal-organic frameworks. Chem. Comm.  51, 4796-4798 (2015)
DOI: 10.1039/c5cc00694e

D. Helmer, I. Rink, J. A. R. Dalton, K. Brahm, M. Jöst, T. M. Nargang, W. Blum, P. Wadhwani, G. Brenner-Weiss, B. E. Rapp, J. Giraldo and K. Schmitz. Rational design of a peptide capture agent for CXCL8 based on a model of the CXCL8:CXCR1 complex. RSC Advances 5, 25657-25668 (2015)
DOI:10.1039/C4RA13749C

V. Kubyshkin, S. Afonin, S. Kara, N. Budisa, P. K. Mykhailiuk and A. S. Ulrich. gamma-(S)-Trifluoromethyl proline: Evaluation as a structural substitute of proline for solid state 19F-NMR peptide studies. Org. Biomol. Chem. 13, 3171-3181 (2015)
DOI:10.1039/C5OB00034C

G. Manzo, M. A. Scorciapino, P. Wadhwani, J. Bürck, N. P. Montaldo, M. Pintus, R. Sanna, M. Casu, A. Giuliani, G. Pirri, V. Luca, A. S. Ulrich and A. C. Rinaldi. Enhanced amphiphilic profile of a short ß-stranded peptide improves its antimicrobial activity. PLoS One 10, e0116379 (2015)
DOI:10.1371/journal.pone.0116379

J. Misiewicz, S. Afonin, S. L. Grage, J. van den Berg, E. Strandberg, P. Wadhwani and A. S. Ulrich. Action of the multifunctional peptide BP100 on native biomembranes examined by solid-state NMR. J. Biomol. NMR 61, 287-298 (2015)
DOI:10.1007/s10858-015-9897-8

J. Misiewicz, S. Afonin and A. S. Ulrich. Control and role of pH in peptide-lipid interactions in oriented membrane samples. Biochim. Biophys. Acta - Biomembranes 1848, 833-841 (2015)
DOI:10.1016/j.bbamem.2014.12.006

J.-D. Savoie, F. Otis, J. Bürck, A. S. Ulrich and N. Voyer. Crown ether helical peptides are preferentially inserted in lipid bilayers as a transmembrane ion channels. Biopolymers 104, 427-433 (2015)
DOI:10.1002/bip.22633

T. Serdiuk, I. Bakanovich, V. Lysenko, S. A. Alekseev, V. A. Skryshevsky, S. Afonin, E. Berger, A. Geloen and I. V. Komarov. Delivery of SiC-based nanoparticles into live cells driven by cell-penetrating peptides SAP and SAP-E. RSC Advances 5, 20498-20502 (2015)
DOI:10.1039/C4RA10688A

E. Strandberg, A. S. Ulrich. AMPs and OMPs: Is the folding and bilayer insertion of b-stranded outer membrane proteins governed by the same biophysical principles as for a-helical antimicrobial peptides? Biochim. Biophys. Acta - Biomembranes 1848, 1944-1954 (2015)
DOI:10.1016/j.bbamem.2015.02.019

E. Strandberg, J. Zerweck, D. Horn, G. Pritz, M. Berditsch, J. Bürck, P. Wadhwani and A. S. Ulrich. Influence of hydrophobic residues on the activity of the antimicrobial peptide magainin 2 and its synergy with PGLa. J. Pept. Sci. 21, 436-445 (2015)
DOI:10.1002/psc.2780

B. A. Wallace, J. Bürck. Third international synchrotron radiation circular dichroism spectroscopy meeting. Synchrotron Radiation News 28, 58-59 (2015)
DOI:10.1080/08940886.2015.1059247

D. Windisch, C. Ziegler, S. L. Grage, J. Bürck, M. Zeitler, P. L. Gor'kov, A. S. Ulrich. Hydrophobic mismatch drives the interaction of E5 with the transmembrane segment of PDGF receptor. Biophys. J. 109, 737-749 (2015)
DOI:10.1016/j.bpj.2015.07.022

H. Zamora-Carreras, B. Maestro, E. Strandberg, A. S. Ulrich, J. M. Sanz and M. Ángeles Jiménez. Micelle-triggered ß-hairpin to a-helix transition in a 14-residue peptide from a choline-binding repeat of the pneumococcal autolysin LytA. Chemistry - A European Journal 21, 8076-8089 (2015)
DOI:10.1002/chem.201500447

D. Aberle, C. Muhle-Goll, J. Bürck, M. Wolf, S. Reißer, B. Luy, W. Wenzel, A. S. Ulrich, G. Meyers. Structure of the membrane anchor of pestivirus glycoprotein E_rns, a long tilted amphipathic helix. PLoS Pathogenes 10, e1003973 (2014)

DOI: 10.1371/journal.ppat.1003973

S. Afonin, R. W. Glaser, C. Sachse, J. Salgado, P. Wadhwani, A. S. Ulrich. 19F NMR screening of unrelated antimicrobial peptides shows that membrane interactions are largely governed by lipids. Biochim. Biophys. Acta - Biomembranes 1838, 2260-2268 (2014)

DOI: 10.1016/j.bbamem.2014.03.017

O. Babii, S. Afonin, M. Berditsch, S. Reiβer S, P. K. Mykhailiuk, V. S. Kubyshkin, T. Steinbrecher, A. S. Ulrich, I. V. Komarov. Controlling biological activity with light: diarylethene-containing cyclic peptidomimetics. Angewandte Chem. Intl. Ed. 53, 3392-3395 (2014) and Angewandte Chemie 126, 3460-3463 (2014)

DOI: 10.1002/anie.201310019 and 10.1002/ange.201310019

C. G. Cranfield, B. A. Cornell, S. L. Grage, P. Duckworth, S. Carne, A. S. Ulrich, B. Martinac. Transient potential gradients and impedance measures of tethered bilayer lipid membranes: Pore-forming peptide insertion and the effect of electroporation. Biophys. J. 106, 182-189 (2014)

DOI: 10.1016/j.bpj.2013.11.1121

S. Fanghänel, P. Wadhwani, E. Strandberg, W. P. Verdurmen, J. Bürck, S. Ehni, P. K. Mykhailiuk, S. Afonin, D. Gerthsen, I. V. Komarov, R. Brock, A. S. Ulrich. Structure analysis and conformational transitions of the cell penetrating peptide transportan 10 in the membrane-bound state. PLoS ONE 9, e99653 (2014)

DOI: 10.1371/journal.pone.0099653

U. I. M. Gerling, M. Salwiczek, C. D. Cadicamo, H. Erdbrink, C. Czekelius, S. L. Grage, P. Wadhwani, A. S. Ulrich, M. Behrends, G. Haufe, B. Koksch. Fluorinated amino acids in amyloid formation: A symphony of size, hydrophobicity and α-helix propensity. Chem. Sci. 5, 819-830 (2014)

DOI: 10.1039/C3SC52932K

M. Girrbach, I. Meliciani, B. Waterkotte, S. Berthold, A. Oster, F. Brurein, T. Strunk, P. Wadhwani, S. Berensmeier, W. Wenzel, K. Schmitz. A fluorescence polarization assay for the experimental validation of an in silico model of the chemokine CXCL8 binding to receptor-derived peptides. Phys. Chem. Chem. Phys. 16, 8036-8043 (2014)

DOI: 10.1039/c3cp53850h

S. L. Grage, X. Xu, M. Schmitt, P. Wadhwani, A. S. Ulrich. 19F-labeling of peptides revealing long-range NMR distances in fluid membranes. J. Phys. Chem. Lett. 5, 4256-4259 (2014)

DOI: 10.1021/jz502195t

W. Grosse, G. Psakis, B. Mertins, P. Reiss, D. Windisch, F. Brademann, J. Bürck, A. S. Ulrich, U. Koert, L. O. Essen. Structure-based engineering of a minimal porin reveals loop-independent channel closure. Biochem. 53, 4826-4838 (2014)

DOI: 10.1021/bi500660q

Z. G. Gu, J. Bürck, A. Bihlmeier, J. Liu, O. Shekhah, P. G. Weidler, C. Azucena, Z. Wang, S. Heissler, H. Gliemann, W. Klopper, A. S. Ulrich, C. Wöll C. Oriented circular dichroism analysis of chiral surface-anchored metal-organic frameworks grown by liquid-phase epitaxy and upon loading with chiral guest compounds. Chemistry 20, 9879-9882 (2014)

DOI: 10.1002/chem.201402567

J. Podlech, S. C. Fleck, M. Metzler, J. Bürck, A. S. Ulrich. Determination of the absolute configuration of perylene quinone-derived mycotoxins by measurement and calculation of electronic circular dichroism spectra and specific rotations. Chemistry 20, 11463-11470 (2014)

DOI: 10.1002/chem.201402567

S. Reißer, E. Strandberg, T. Steinbrecher, A. S. Ulrich. 3D hydrophobic moment vectors as a tool to characterize the surface polarity of amphiphilic peptides. Biophys. J. 106, 2385-2394 (2014)

DOI: 10.1016/j.bpj.2014.04.020

S. Ruskamo, R. P. Yadav, S. Sharma, M. Lehtimäki, S. Laulumaa, S. Aggarwal, M. Simons, J. Bürck, A. S. Ulrich, A. H. Juffer, I. Kursula, P. Kursula. Atomic resolution view into the structure-function relationships of the human myelin peripheral membrane protein P2. Acta Cryst. D 70, 165-176 (2014)

DOI: 10.1107/S1399004713027910

L. A. Sommer, J. J. Janke, W. F. Bennett, J. Bürck, A. S. Ulrich, D. P. Tieleman, S. A. Dames. Characterization of the immersion properties of the peripheral membrane anchor of the FATC domain of the kinase "target of rapamycin" by NMR, oriented CD spectroscopy, and MD simulations. J. Phys. Chem. B 118, 4817-4831 (2014)

DOI: 10.1021/jp501533d

E. Strandberg, A. S. Ulrich. Dynamic structure analysis of peptides in membranes by solid-state NMR. In "Advances in Biological Solid-State NMR: Proteins and Membrane-Active Peptides”, Topics in Current Chemistry, Book 306, pages 304-319, Editors: F. Separovic, A. Naito, Royal Society of Chemistry (2014)

ISBN: 9781849739108

http://pubs.rsc.org/en/content/ebook/978-1-84973-910-8#!divbookcontent

A. N. Tkachenko, P. K. Mykhailiuk, D. S. Radchenko, O. Babii, S. Afonin, A. S. Ulrich, I. V. Komarov. Design and synthesis of a monofluoro-substituted aromatic amino acid as a conformationally restricted 19F NMR label for membrane-bound peptides. Eur. J. Org. Chem. 2014, 3584-3591 (2014)

DOI: 10.1002/ejoc.201301737

D. Volz, M. Wallesch, S. L. Grage, J. Göttlicher, R. Steininger, D. Batchelor, T. Vitova, A. S. Ulrich, C. Heske, L. Weinhardt, T. Baumann, S. Bräse. Labile or stable: Can homoleptic and heteroleptic pyrphos-copper complexes be processed from solution? Inorg. Chem. 53, 7837-7847 (2014)

DOI: 10.1021/ic500135m

P. Wadhwani, E. Strandberg, J. van den Berg, C. Mink, J. Bürck, R. A. Ciriello, A. S. Ulrich. Dynamical structure of the short multifunctional peptide BP100 in membranes. Biochim. Biophys. Acta - Biomembranes 1838, 940-949 (2014)

DOI: 10.1016/j.bbamem.2013.11.001

T. H. Walther, A. S. Ulrich. Transmembrane helix assembly and the role of salt bridges. Curr. Op.Struct. Biol. 27, 63-68 (2014)

DOI: 10.1016/j.sbi.2014.05.003

Y. Wang, T. Zhao, D. Wei, E. Strandberg, A. S. Ulrich, J. P. Ulmschneider. How reliable are molecular dynamics simulations of membrane active antimicrobial peptides? Biochim. Biophys. Acta - Biomembranes 1838, 2280-2288

DOI: 10.1016/j.bbamem.2014.04.009

D. Windisch, C. Ziegler, J. Bürck, A. S. Ulrich. Structural characterization of a C-terminally truncated E5 oncoprotein from papillomavirus in lipid bilayers. Biol. Chem. 395, 1443-1452 (2014)

DOI: 10.1515/hsz-2014-0222

2004:

• U.Lauf, A.Fahr, K.Westesen, A.S.Ulrich
  Novel lipid-nanotubes in dispersions of DMPC
  Chem. Phys. Chem. 2004; 5: 1246-1249
  
   
• E.Strandberg, A.S.Ulrich
  NMR methods for studying membrane-active antimicrobial peptides
  Concepts Magn. Res. 2004; 23A: 89-120
  
   
• S.Grage, S.Afonin, M.Grüne, A.S.Ulrich
  Interaction of the fusogenic peptide B18 in its amyloid-state with DMPC bilayers studied by solid-state ²H- and ³¹P-NMR and DSC
  Chem. Phys. Lipids 2004; 132: 65-77
  
   
• R. W. Glaser, C. Sachse, U. H. N. Dürr, P. Wadhwani, A.S.Ulrich
  Orientation of the antimicrobial peptide PGLa in lipid membranes determined from ¹⁹F-NMR dipolar couplings of 4-CF₃-phenylglycine labels
  J. Mag. Res. 2004; 168: 153-163
  
   
• S.Afonin, U.H.N.Dürr, R.W.Glaser, A.S.Ulrich
  "Boomerang"-like insertion of a fusogenic peptide in a lipid membrane revealed by solid state ¹⁹F NMR
  Mag. Res. Chem. 2004; 42: 195-203
  
   
• T.Asakura, K.Suita, T.Kameda, S.Afonin, A.S.Ulrich
  Structural role of tyrosine in Bombyx mori silk fibroin, studied by solid-state NMR and molecular mechanics on a model peptide prepared as silk I and II
   Mag. Res. Chem. 2004; 42: 258-266
  
   
• O.Toke, R. D.O’Connor, T.K.Weldeghiorghis, W.L.Maloy, R.W.Glaser, A.S.Ulrich, J.Schaefer

  Structure of (KIAGKIA)₃ aggregates in phospholipid bilayers by solid-state NMR.
  Biophys. J. 2004; 87: 675-678
   

• P.Wadhwani, U.L.H.Dürr,S.Afonin, R.W.Glaser, E.Strandberg, P.Tremouilhac, C.Sachse, M.Berditchevskaja, S.Grage, R.Eisenhuth, D.Maisch, A.S.Ulrich
  Solid-state ¹⁹F-NMR analysis of membrane-active peptides
  Book Chapter
   
• U. Sternberg, R. Witter, A.S.Ulrich
  3D Structure elucidation using NMR Chemical Shifts
  Ann. Rep. on NMR 2004; 52: 53-104
  
  
  
  2003:
   

   

• S.Afonin, R.W.Glaser, M.Berditchevskaja, P.Wadhwani, K.H.Gührs, U.Möllmann, A.S.Ulrich
  4-Fluoro-phenylglycine as a label for ¹⁹F-NMR structure analysis of membrane-associated peptides
  Chem. Bio. Chem 2003; 4: 1151-1163
  
   
• U. Sternberg, F.-T. Koch, W. Prieß, R. Witter
  Crystal Structure Refinements of Cellulose Polymorphs using solid state ¹³C Chemical Shifts
  Cellulose 2003; 10: 189-199
   
• R.W.Glaser, A.S.Ulrich
  Susceptibility corrections in solid-state NMR experiments with macroscopically oriented membrane samples. Part I: Applications
  J. Mag. Res. 2003; 164: 104-114
  
   
• R.Ulrich, R.W.Glaser, A.S.Ulrich
  Susceptibility corrections in solid-state NMR experiments with macroscopically oriented membrane samples. Part II: Theory
  J. Mag. Res. 2003; 164: 115-127
  
   
• R.Witter, St.Hesse, and U.Sternberg
  Powder Pattern Recoupling at 10 kHz Spinning Speed Applied to Cellulose
  J. Magn. Reson. 2003; 161: 35-42
  
  
  
  2002:
   
• A.S.Ulrich
  Biophysical aspects of using liposomes as delivery vehicles
  Bioscience Reports 2002; 22: 129-150
  
   
• S.L.Grage, J.Wang, T.A.Cross, A.S.Ulrich
  Structure analysis of fluorine-labelled tryptophan side-chains in gramicidin A by solid state ¹⁹F-NMR
  Biophys. J. 2002; 83: 3336-3350
  
   
• T.Asakura, J.Yao, T.Yamane, K.Umemura, A.S.Ulrich
  Heterogeneous structure of silk fibers from Bombyx mori resolved by ¹³C solid-state NMR spectroscopy
  J. Am. Chem. Soc. 2002; 124: 8794-8795
  
   
• Witter, W. Prieß, U. Sternberg
  Chemical Shift Driven Geometry Optimization
  J. Comp. Chem. 2002; 23: 298-305
  
   

   

  2001:

• J.Salgado, S.L.Grage, L.H.Kondejewski, R.N.McElhany, R.S.Hodges, A.S.Ulrich
  Alignment of the antimicrobial β-sheet peptide gramicidin S in membranes: a solid state ¹⁹F-NMR study in oriented lipid bilayers
  J. Biomol. NMR 2001; 21: 191-208
   
• J.Salgado, S.L.Grage, L.H.Kondejewski, R.S. Hodges, R.N.McElhany, A.S.Ulrich
  Membrane-bound structure and alignment of the antimicrobial β-sheet peptide gramicidin S derived from angular and distance constraints by solid state ¹⁹F-NMR
  J. Biomol. NMR 2001; : 1-18
  
   
• S.L.Grage, J.Salgado, U.H.N.Dürr, S.Afonin, R.W.Glaser, A.S.Ulrich
  Solid state ¹⁹F-NMR of biomembranes
  In "Perspectives on Solid State NMR in Biology" (Eds. S.Kiihne, H.J.M.de Groot), Kluwers Academic Press: 83-91
   
• Y.Hori, M.Demura, M.Iwadate, A.S.Ulrich, T.Niidome, H.Aoyagi, T.Asakura
  Interaction of mastoparan with membranes studied by ¹H-NMR in detergent micelles and by solid state ²H- and ¹⁵N-NMR in oriented lipid bilayers
  Eur. J. Biochem. 2001; 268: 302-309
  
   
• H.Binder, K.Arnold, A.S.Ulrich O.Zschörnig
  Interaction of Zn²⁺ with phospholipid membranes
  Biophys. Chem. 2001; 90: 57-74
  
   
• T.Heinze, A.Koschella, L.Magdaleno, A.S.Ulrich
  Nucleophilic displacement reactions on tosyl cellulose by chiral amines
  Polymer Bull. 2001; 46: 7-13

   

  2000:
   

• A.S.Ulrich
  High resolution ¹H and ¹⁹F solid state NMR
  In "Encyclopedia of Spectroscopy and Spectrometry" (Eds. J.Lindon, G.Tranter, J.Holmes), Academic Press 2000: 813-825
  
   
• S.L.Grage, A.S.Ulrich
  Orientation-dependent ¹⁹F dipolar couplings within a trifluoromethyl-group are revealed by multipulse solid state NMR
  J. Mag. Res. 2000; 146: 81-88
  
   
• H.Binder, K.Arnold, A.S.Ulrich, O.Zschörnig
  The effect of Zn²⁺ on the secondary structure of a histidine-rich fusogenic peptide and its interaction with lipid membranes
  Biochim. Biophys. Acta 2000; 1468: 345-358
  
   
• S.L.Grage, D.Gauger, C.Selle, W.Pohle, W.Richter, A.S.Ulrich
  The amphiphilic drug flufenamic acid can induce hexagonal lipid phases in DMPC - a ³¹P and ¹⁹F-NMR study
  Phys. Chem. Chem. Phys. 2000; 2: 4574-4579
   
• H.W.Meyer, K.Semmler, W.Rettig, W.Pohle, A.S.Ulrich, S.L.Grage, C.Selle, F.Richter, P.Quinn
  Hydration of DMPC and DPPC at 4°C produces a novel gel phase with convex-concave bilayer curvatures
  Chem. Phys. Lipids 2000; 105: 149-166

   

  1999:
   

• S.L.Grage, A.S.Ulrich
  Structural parameters from ¹⁹F homonuclear dipolar couplings, obtained by multipulse solid state NMR in static oriented systems
  J. Mag. Res. 1999; 138: 98-106
  
   
• A.S.Ulrich, W.Tichelaar, G.Förster, O.Zschörnig, S.Weinkauf, H.W.Meyer
  Ultrastructural characterization of peptide-induced membrane fusion and peptide self-assembly in the bilayer
  Biophys. J. 1999; 77: 829-841
  
   
• R.W.Glaser, M.Grüne, C.Wandelt, A.S.Ulrich
  NMR and CD structural analysis of the fusogenic peptide sequence B18 from the fertilization protein bindin
  Biochemistry 1999; 38: 2560-2569
  
   
• T.Kameda, Y.Ohkawa, K.Yoshizawa, J.Naito, A.S.Ulrich, T.Asakura
  Hydrogen-bonding in serine side chains of Bombyx mori and Samia cynthia ricinisilk fibroins using solid state ²H-NMR
  Macromol. 1999; 32: 7166-7171
  
   
• T.Kameda, Y.Ohkawa, K.Yoshizawa, J.Nakano, A.S.Ulrich, T.Asakura
  Dynamics of the tyrosine side chains of Bombyx mori and Samia cynthia ricinisilk fibroins using solid state ²H-NMR
  Macromol. 1999; 32: 8491-8495
  
   
• H.W.Meyer, H.Bunjes, A.S.Ulrich
  Morphological transitions of brain sphingomyelin are determined by the hydration protocol: ripples re-arrange in plane, and sponge-like networks disintegrate into small vesicles
  Chem. Phys. Lipids 1999; 99: 111-123
   
• A.S.Ulrich, A.Watts
  Solid state ²H-NMR of lipids and proteins, complemented by neutron diffraction
  In "Deuteration of Biological Macromolecules" (Ed. I.N.Serdyuk), JINR Publishing 1999: 57-60
   
• A.S.Ulrich
  Wissenschaft als Beruf
  Forschung & Lehre 1999; 5: 238-241

   

  1998:
   

• A.S.Ulrich, S.L.Grage.
  In "Solid state NMR on polymers" (Eds. I.Ando, T.Asakura), Elsevier, Amsterdam1998: 190-211
   
• A.S.Ulrich, M.Otter, C.Glabe, D.Hoekstra
  Membrane fusion is triggered by a distinct peptide sequence of the sea urchin fertilization protein bindin
  J. Biol. Chem. 1998; 273: 16748-16755
  
   
• H.W.Meyer, M.Westermann, W.Richter, M.Stumpf, A.S.Ulrich, C.Hoischen
  Minimal radius of curvature of lipid bilayers in the gel state corresponds to the dimension of bimembrane structures "cavaeolae"
  J. Struct. Biol. 1998; 124: 77-87
   
•  A.S.Ulrich, S.L.Grage, M.Demura, T.Asakura
  2H-Labelling of silk fibroin fibers and their structural characterization by solid state ²H-NMR
  In "Internl. Symposium on Silk and NMR" 1998: 35-41
   
• A.S.Ulrich
  Membranfusion
  Chemie Heute 98/99: 113-115

   

  1997:
  
   

• H.Patzelt, A.S.Ulrich,P.Düx, H.Egbringhoff, J.Ashurst, H.Oschkinat, D.Oesterhelt
  Towards structural investigations on isotope labelled native bacteriorhodopsin in detergent micelles by solution-state NMR spectroscopy
  J. Biomol. NMR 1997; 10: 95-106
  
   
• T.Asakura, M.Minami, R.Shimada, M.Demura, M.Osanai, T.Fujito, M.Imanari, A.S.Ulrich
  ²H-labeling of silk fibroin fibers and their structural characterization by solid-state ²H NMR
  Macromol. 1997; 30: 2429-2435
  

   

  1996:
  
   

• A.Loidl-Stahlhofen, A.S.Ulrich, S.Kaufmann, T.M.Bayerl
  Protein binding to lipid bilayers controlled by the lipid phase state and mixing behaviour: a new concept for highly selective protein purification
  Eur. Biophys. J. 1996; 25: 151-153
   
• A.S.Ulrich
  ²H-NMR studies of oriented membranes to determine single bond orientations
  Macromol. Symp. 1996; 101: 81-89
   
• M.Demura, M.Minami, T.Asakura, A.S.Ulrich
  Dynamics conformation of uniaxially orientated silk fibroin fiber studied with solid state ²H-NMR
  Prog. Polymer Physics 1996; 39: 1-4

   

   

  until 1995:
  
   

• Ulrich, A.S., I.Wallat, M.P. Heyn, A.Watts
  Re-alignment of the retinal chromophore in the M-state of bacteriorhodopsin
  Nature Struct. Biol. 1995; 2: 190-192
   
• Watts, A., A.S.Ulrich, D.A.Middleton
  Solid-state NMR studies of membrane proteins (Review)
  Mol. Membr. Biol. 1995; 12: 233-246
   
• Ulrich, A.S., A.Watts, I.Wallat, M.P.Heyn
  Distorted structure of the retinal chromophore in bacteriorhodopsin resolved by ²H-NMR
  Biochem. 1994; 33: 5370-5375
   
• Ulrich, A.S., A.Watts
  Molecular response of the lipid headgroup to bilayer hydration as monitored by ²H-NMR
  Biophys. J. 1994; 66: 1441-1449
   
• Ulrich, A.S., A.Watts
  Lipid headgroup hydration studied by ²H-NMR: a link between spectroscopy and thermodynamics
  Biophys. Chem. 1994; 49: 39-50
   
• Ulrich, A.S., M.Sami, A.Watts
  Hydration of DOPC bilayers by differential scanning calorimetry
  Biochim. Biophys. Acta 1994; 1191: 225-230
   
• Watts, A., B.Sternberg, A.S.Ulrich, C.J.Whiteway, G.Seifert, M.Sami, P.Fisher, M.P.Heyn, I.Wallat
  Bacteriorhodopsin: the effect of bilayer thickness on 2D-array formation, and the structural re-alignment of retinal through the photocycle
  Biophys. Chem. 1993; 56: 41-46
   
• Ulrich, A.S., A.Watts
  ²H-NMR lineshapes of immobilized uniaxially oriented membrane proteins
  Solid State NMR 1993; 2: 21-36
   
• Ulrich, A.S., M.P. Heyn, A.Watts
  Structure determination of the cyclohexene-ring of retinal in bacteriorhodopsin by solid-state deuterium-NMR
  Biochem. 1992; 31: 10390-10399
   
• Ulrich, A.S., I.Wallat, M.P.Heyn, A.Watts
  Evidence for a curved retinal chain in bacteriorhodopsin from solid-state deuterium-NMR
  In "Structures and Functions of Retinal Proteins" (ed. J.L. Rigaud), John Libbey Eurotext 1992: 247-250
   
• Ulrich, A.S., A.Watts
  Membrane protein structure determination by deuterium-NMR
  In "Structure, Biogenesis and Dynamics of Biological Membranes" (ed. J.A.F. Op den Kamp), NATO series 1991; Vol. H 63: 243-249
   
• Ulrich, A.S., F.Volke, A.Watts
  The dependence of phospholipid headgroup mobility on hydration asstudied by ²H-NMR spin lattice relaxation time measurements
  Chem. Phys. Lipids 1990; 55: 61-66
   
• Ulrich, A.S., T.Poile, A.Watts
  Deuterium NMR to study the surface of phospholipid bilayers
  Bull. Magn. Reson. 1990; 12: 80-83
   
• Blake-Coleman, B.C., A.S.Ulrich, P.Fitzpatrick, M.R.Calder, D.J.Clarke
  Apparatus for the electrical characterization of conductive fluids
  Biosensors 1989; 4: 87-108