Oxpholipin 11D: an anti-inflammatory peptide that binds cholesterol and oxidized phospholipids.

ABSTRACT:

Background

Many gram-positive bacteria produce pore-forming exotoxins that contain a highly conserved, 12-residue domain (ECTGLAWEWWRT) that binds cholesterol. This domain is usually flanked N-terminally by arginine and C-terminally by valine. We used this 14-residue sequence as a template to create a small library of peptides that bind cholesterol and other lipids.

Methodology/results

Several of these peptides manifested anti-inflammatory properties in a predictive in vitro monocyte chemotactic assay, and some also diminished the pro-inflammatory effects of low-density lipoprotein in apoE-deficient mice. The most potent analog, Oxpholipin-11D (OxP-11D), contained D-amino acids exclusively and was identical to the 14-residue design template except that diphenylalanine replac

SUBMITTER: Ruchala P 

PROVIDER: S-EPMC2854715 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature