1xv7
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Solution structure of antimicrobial and endotoxin-neutralizing peptide Lf11 in DPC micelles
OverviewOverview
Treatment of Gram-negative bacterial infections with antimicrobial agents, can cause release of the endotoxin lipopolysaccharide (LPS), the potent, initiator of sepsis, which is the major cause of mortality in intensive, care units worldwide. Structural information on peptides bound to LPS can, lead to the development of more effective endotoxin neutralizers. Short, linear antimicrobial and endotoxin-neutralizing peptide LF11, based on the, human lactoferrin, binds to LPS, inducing a peptide fold with a "T-shaped", arrangement of a hydrophobic core and two clusters of basic residues that, match the distance between the two phosphate groups of LPS. Side chain, arrangement of LF11 bound to LPS extends the previously proposed LPS, binding pattern, emphasizing the importance of both electrostatic and, hydrophobic interactions in a defined geometric arrangement. In anionic, micelles, the LF11 forms amphipathic conformation with a smaller, hydrophobic core than in LPS, whereas in zwitterionic micelles, the, structure is even less defined. Protection of tryptophan fluorescence, quenching in the order SDS>LPS>DPC and hydrogen exchange protection, indicates the decreasing extent of insertion of the N terminus and, potential role of peptide plasticity in differentiation between bacterial, and eukaryotic membranes.
About this StructureAbout this Structure
1XV7 is a Protein complex structure of sequences from [1] with NH2 as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structural origin of endotoxin neutralization and antimicrobial activity of a lactoferrin-based peptide., Japelj B, Pristovsek P, Majerle A, Jerala R, J Biol Chem. 2005 Apr 29;280(17):16955-61. Epub 2005 Feb 1. PMID:15687491
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