S
Sergii Afonin
Researcher at Karlsruhe Institute of Technology
Publications - 99
Citations - 3203
Sergii Afonin is an academic researcher from Karlsruhe Institute of Technology. The author has contributed to research in topics: Peptide & Lipid bilayer. The author has an hindex of 32, co-authored 93 publications receiving 2794 citations. Previous affiliations of Sergii Afonin include University of Jena.
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Journal ArticleDOI
Chemical labeling strategy with (R)- and (S)-trifluoromethylalanine for solid state 19F NMR analysis of peptaibols in membranes.
TL;DR: The new (19)F NMR label CF(3)-Ala has thus been demonstrated to be highly sensitive, virtually unperturbing, and ideally suited to characterize peptaibols in membranes.
Journal ArticleDOI
γ-(S)-Trifluoromethyl proline: evaluation as a structural substitute of proline for solid state 19F-NMR peptide studies
Vladimir Kubyshkin,Vladimir Kubyshkin,Sergii Afonin,Sezgin Kara,Nediljko Budisa,Pavel K. Mykhailiuk,Pavel K. Mykhailiuk,Anne S. Ulrich +7 more
TL;DR: The exchange of native proline for γ-trifluoromethyl proline in the peptide antibiotic gramicidin S was shown to preserve the overall amphipathic peptide structure and the utility of the amino acid as a selective (19)F-NMR label was demonstrated.
Journal ArticleDOI
19F NMR Analysis of the Antimicrobial Peptide PGLa Bound to Native Cell Membranes from Bacterial Protoplasts and Human Erythrocytes
TL;DR: The characteristic fingerprint splitting of its (19)F reporter group indicated that the peptide helix binds to the native membranes in a surface alignment, albeit with a higher affinity in the prokaryotic than the eukaryotic system.
Book ChapterDOI
Solid State NMR Structure Analysis of the Antimicrobial Peptide Gramicidin S in Lipid Membranes: Concentration-Dependent Re-alignment and Self-Assembly as a β-Barrel.
TL;DR: Orientational NMR constraints suggest that the peptide may self-assemble as an oligomeric β-barrel pore, which is stabilized by intermolecular hydrogen bonds, based on the oligomersic structural model and the conditions of pore formation.
Journal ArticleDOI
Structure Analysis and Conformational Transitions of the Cell Penetrating Peptide Transportan 10 in the Membrane-Bound State
Susanne Fanghänel,Parvesh Wadhwani,Erik Strandberg,Wouter P. R. Verdurmen,Jochen Bürck,Sebastian Ehni,Pavel K. Mykhailiuk,Sergii Afonin,Dagmar Gerthsen,Igor V. Komarov,Roland Brock,Anne S. Ulrich +11 more
TL;DR: The cross-talk between the two regions of TP10 exerts a delicate balance on its conformational switch, as the presence of the α-helix counteracts the tendency of the unfolded N-terminus to self-assemble into β-pleated fibrils.