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Conformational study of melectin and antapin antimicrobial peptides in model membrane environments.
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
Cocaine Hydrochloride Structure in Solution Revealed by Three Chiroptical Methods.
The spectroscopic results and computational analysis are consistent with X-ray structures of known cocaine-receptor complexes, in which the compound adopts a variety of conformations. 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
Reply to Comments by Pescitelli and Bruhn on "Cocaine Hydrochloride Structure in Solution Revealed by Three Chiroptical Methods".
Viewed from certain perspective, the Correspondence itself shows that ECD may be quite problematic, but the authors are certainly right that the techniques are complementary and one should not dig arbitrary ditches between them. Expand