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Conformational study of melectin and antapin antimicrobial peptides in model membrane environments.
TLDR
A significant content of α-helical conformation is found in the solutions of negatively charged liposomes mimicking the bacterial membrane, thus correlating with the antimicrobial activity of the studied peptides. Expand
Key steps in unconventional secretion of fibroblast growth factor 2 reconstituted with purified components
TLDR
The minimal molecular machinery required for FGF2 membrane translocation in a fully reconstituted inside-out vesicle system is defined and a novel type of self-sustained protein translocation across membranes is established, revealing the molecular basis of the unconventional secretory pathway of F GF2. Expand
Panurgines, novel antimicrobial peptides from the venom of communal bee Panurgus calcaratus (Hymenoptera: Andrenidae)
TLDR
Three novel antimicrobial peptides, named panurgines (PNGs), were isolated from the venom of the wild bee Panurgus calcaratus to study the effects of cationicity, amphipathicity, and hydrophobicity on the biological activity. Expand
Interaction of a novel antimicrobial peptide isolated from the venom of solitary bee Colletes daviesanus with phospholipid vesicles and Escherichia coli cells
TLDR
It was found that the studied peptides permeated both the outer and inner cytoplasmic membranes of Escherichia coli, and treatment of E. coli with one of the COD analogs caused leakage of bacterial content mainly from the septal areas of the cells. Expand
Structural Basis for Antimicrobial Activity of Lasiocepsin
TLDR
Lasiocepsin structurally belongs to the ShK family and shows a strong preference for anionic phospholipids; this is further augmented by increasing concentrations of cardiolipin, such as those found at the poles of bacterial cells. Expand
Vibrational and electronic circular dichroism as powerful tools for the conformational analysis of cationic antimicrobial peptides
Antimicrobial and hemolytic activities of cationic α-helical antimicrobial peptides depend on their ability to adopt an amphipathic α-helical conformation on the cell membrane surface. UsingExpand
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