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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Peptoidic Amino- and Guanidinium-Carrier Systems: Targeted Drug Delivery into the Cell Cytosol or the Nucleus
TL;DR: In this paper, carrier-peptoids with either amino or guanidinium side chains were investigated with regard to their cellular uptake, toxicity, and intracellular localization.
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Coding and decoding libraries of sequence-defined functional copolymers synthesized via photoligation
Nicolas Zydziak,Waldemar Konrad,Florian Feist,Sergii Afonin,Steffen M. Weidner,Christopher Barner-Kowollik +5 more
TL;DR: It is submitted that the presented photochemical strategy is a viable and advanced concept for coding individual monomer units along a macromolecular chain and the in-depth characterization of each sequence-defined chain confirms the precision nature of the macromolescules.
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Conformationally Rigid Trifluoromethyl‐Substituted α‐Amino Acid Designed for Peptide Structure Analysis by Solid‐State 19F NMR Spectroscopy
Pavel K. Mikhailiuk,Pavel K. Mikhailiuk,Sergii Afonin,Alexander N. Chernega,Eduard B. Rusanov,M. O. Platonov,M. O. Platonov,G. G. Dubinina,G. G. Dubinina,Marina Berditsch,Anne S. Ulrich,Igor V. Komarov,Igor V. Komarov +12 more
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Temperature-dependent transmembrane insertion of the amphiphilic peptide PGLa in lipid bilayers observed by solid state 19F NMR spectroscopy.
TL;DR: The alignment of the antimicrobial peptide PGLa in a lipid bilayer was characterized by solid state 19F NMR on selectively CF3-labeled peptides in oriented samples but as a function of temperature and lipid phase state.
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The cell-penetrating peptide TAT(48-60) induces a non-lamellar phase in DMPC membranes.
Sergii Afonin,Alex Maximilian Frey,Sybille Bayerl,Dahlia Fischer,Parvesh Wadhwani,Sevil Weinkauf,Anne S. Ulrich +6 more
TL;DR: Study of the interaction of the HIV-derived CPP TAT with model membranes by solid-state NMR spectroscopy and electron microscopy indicates that TAT induces the formation of rodlike, presumably inverted micelles in DMPC, which may represent intermediates during the translocation across eukaryotic membranes.