G
Galyna Gorbenko
Researcher at University of Kharkiv
Publications - 99
Citations - 1423
Galyna Gorbenko is an academic researcher from University of Kharkiv. The author has contributed to research in topics: Lipid bilayer & Bilayer. The author has an hindex of 18, co-authored 90 publications receiving 1223 citations.
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The role of lipid-protein interactions in amyloid-type protein fibril formation.
TL;DR: The present review summarizes the principal factors responsible for the enhancement of fibril formation in a membrane environment, viz. structural transformation of polypeptide chain into a partially folded conformation, increase of the local concentration of a protein upon its membrane binding, and aggregation-favoring orientation of the bound protein.
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Binding of Lysozyme to Phospholipid Bilayers: Evidence for Protein Aggregation upon Membrane Association
TL;DR: Electrostatic and hydrophobic protein-lipid interactions can be concluded to modulate the aggregation behavior of lysozyme when bound to lipid bilayers, which may have important implications for protein fibrillogenesis in vivo.
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Cytochrome c Interaction with Cardiolipin/Phosphatidylcholine Model Membranes: Effect of Cardiolipin Protonation
TL;DR: To quantitatively describe cyt c membrane binding, the adsorption model based on scaled particle and double layer theories has been employed, with potential-dependent association constants being treated as a function of acidic phospholipid mole fraction, degree of CL protonation, ionic strength, and surface coverage.
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Lysozyme effect on structural state of model membranes as revealed by pyrene excimerization studies.
TL;DR: Excimer-to-monomer fluorescence intensity ratio has been found to reduce on lysozyme association with lipids, interpreted as indicating decrease in the membrane free volume on formation of both electrostatic and hydrophobic protein-lipid contacts.
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Cholesterol modulates interaction between an amphipathic class A peptide, Ac-18A-NH2, and phosphatidylcholine bilayers.
Masashi Egashira,Galyna Gorbenko,Masafumi Tanaka,Hiroyuki Saito,Julian G. Molotkovsky,Minoru Nakano,Tetsurou Handa +6 more
TL;DR: The fluorescence spectral shift, quantum yield, anisotropy, and acrylamide-quenching of the peptide Trp indicated that in PC:Chol (3:2) LUV, Ac-18A-NH2 was located in a more polar membrane environment with increased motional freedom and greater accessibility to the aqueous medium.