Please use this identifier to cite or link to this item:
|Title:||Human neutrophil peptide 1 variants bearing arginine modified cationic side chains: Effects on membrane partitioning||Authors:||Bonucci, Alessio
|Keywords:||HNP-1 variants Arginine modified side chains Bacterial model membrane Reduced lipid–protein interaction Spectroscopic techniques||Issue Date:||2014||Project:||None||Journal:||BIOPHYSICAL CHEMISTRY||Abstract:||
α-Defensins (e.g. human neutrophil peptides, HNPs) have a broad spectrum bactericidal activity contributing to human innate immunity. The positive charge of amino acid side chains is responsible for the first interaction of cationic antimicrobial peptides with negatively charged bacterial membranes. α-Defensins contain a high content of Arg residues compared to Lys. In this paper, different peptide analogs including substitution of Arg-14 respectively with NG–NG′-asymmetric dimethyl-L-arginine (ADMA), NG–NG′-symmetric dimethyl-L-arginine (SDMA) and Lys (R14K and R15K) variants have been studied to test the role of Arg guanidino group and the localized cationic charge of Lys for interaction with lipidmembranes. Our findings showthat all the variants have a decreased disruptive activity against the bilayer. The methylated analogs show a reduction in membrane partitioning due to the lack of their ability to form hydrogen bonds. Comparison with the native HNP-1 peptide has been discussed.
|Appears in Collections:||Publications|
Show full item record
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.