Journal
CHEMMEDCHEM
Volume 3, Issue 11, Pages 1748-1755Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cmdc.200800209
Keywords
biological activity; drug design; lipopeptides; medicinal chemistry; structure-activity relationships
Categories
Funding
- Fundacio La Marato de TV3
- CICYT [BIO2004-998, CTQ2006-03794/BQU]
- Instituto de Salud Carlos III [CB06_01_0074]
- Generalitat de Catalunya [2005SGR 00662]
- Centro de Investigacion Principe Felipe
- Institute for Research in Biomedicine
- Barcelona Science Park
Ask authors/readers for more resources
Peptides that interact with lipopolysoccharide (LPS) can provide the basis for the development of new antisepsis agents. In this work, several LPS-neutralizing acyl peptides derived from LALF, BPI, and SAP were prepared, structurally characterized, and biologically evaluated. In all cases, peptides with long acyl chains showed greater LPS-neutralizing activities than the original acetylated peptides. Structural analysis of these peptides revealed that N-acylation with long acyl chains promotes the formation of micellar or fibril-like nanostructures, thus proving a correlation between anti-LPS activity and nanostructure formation. The results of this study provide useful structural insight for the future design of new acyl peptides that strongly bind LPS and therefore act as antisepsis drugs. Furthermore, this nanostructure-biological activity correlation can be translated into other therapeutic areas.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available