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Bioactive peptides derived from the Limulus anti‐lipopolysaccharide factor: structure‐activity relationships and formation of mixed peptide/lipid complexes
Author(s) -
Mora Puig,
De La Paz Manuela López,
PérezPayá Enrique
Publication year - 2008
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1033
Subject(s) - peptide , chemistry , circular dichroism , limulus , förster resonance energy transfer , fluorescence , lipid a , biochemistry , amino acid , lipopolysaccharide , target peptide , biophysics , biology , paleontology , physics , quantum mechanics , endocrinology
The design of peptides that would interact and neutralise bacterial endotoxins or LPS could have benefited from the analysis of comparative structure–activity relationships among close‐related analogues. Here, we present a comparative structural characterisation of selected peptides derived from the LALF obtained by single‐amino‐acid replacement, which differ in biological activity. The peptides were characterised in solution using nuclear magnetic resonance, circular dichroism and fluorescence spectroscopies. Membrane mimetic peptide interactions were studied using fluorescence resonance energy transfer with the aid of extrinsic fluorescent probes that allowed the identification of mixed peptide/lipid complexes. Copyright © 2008 European Peptide Society and John Wiley & Sons, Ltd.