Enhancement of endotoxin neutralization by coupling of a C12-alkyl chain to a lactoferricin-derived peptide

Enhancement of endotoxin neutralization by coupling of a C12-alkyl chain to a lactoferricin-derived peptide

Antibacterial peptide acylation, which mimics the structure of the natural lipopeptide polymyxin B, increases antimicrobial and endotoxin-neutralizing activities. The interaction of the lactoferricin-derived peptide LF11 and its N-terminally acylated analogue, lauryl-LF11, with different chemotypes...

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Bibliographic Details
Main Authors: Andrä, J. (Jörg), Lohner, K. (Karl), Blondelle, S.E. (Sylvie E.), Jerala, R. (Roman), Moriyon, I. (Ignacio), Koch, M.H.J. (Michel H. J.), Garidel, P. (Patrick), Brandenburg, K. (Klaus)
Format: info:eu-repo/semantics/article
Language:eng
Published: Portland Press 2013
Subjects:
Antimicrobial peptide
Antisepsis
Endotoxin
Hydrophobic extension
Lactoferricin
Lipopolysaccharide
Online Access:https://hdl.handle.net/10171/29428

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