Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/6423
Title: Human neutrophil peptide 1 variants bearing arginine modified cationic side chains: Effects on membrane partitioning
Authors: Bonucci, Alessio
Enrico, Balducci
Manuele, Martinelli
Pogni, Rebecca 
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.
Description: 
76608
URI: http://hdl.handle.net/20.500.12779/6423
ISSN: 0301-4622
DOI: 10.1016/j.bpc.2014.04.003
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