Probing Membrane Topology of the Antimicrobial Peptide Distinctin by Solid-State NMR Spectroscopy in Zwitterionic and Charged Lipid Bilayers

Distinctin is a 47-residue antimicrobial peptide, which interacts with negatively charged membranes and is active against Gram-positive and Gram-negative bacteria. Its primary sequence comprises two linear chains of 22 (chain 1) and 25 (chain 2) residues, linked by a disulfide bridge between Cys19 o...

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Main Authors: Verardi, Raffaello, Traaseth, Nathaniel J., Shi, Lei, Porcelli, Fernando, Monfregola, Luca, De Luca, Stefania, Amodeo, Pietro, Veglia, Gianluigi, Scaloni, Andrea
Formato: Artigo
Idioma:Inglês
Publicado em: 2010
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Article
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2997851/
https://ncbi.nlm.nih.gov/pubmed/20719234
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bbamem.2010.08.008
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