Selection of Mac-1 Inhibitors by Phage Display

Neutrophil recruitment to sites of inflammation is necessary for repair of damaged tissue, but in sprocess may lead to further damage of the involved tissue. The action of Mac-1, an adhesion moleculesurface of neutrophils, is required for neutrophil recruitment during the inflammatory response. Ituseful to inhibit the action of Mac-1 on neutrophils for the treatment of acute inflammatory conditirespiratory distress syndrome, stroke, inflammatory bowel disease, and ischemia-reperfusion injury.peptide which inhibits Mac-1 mediated neutrophil adherence in vitro, with an IC5O of 2 micromoles. Odevelop a more potent version of this Mac-1 antagonist through phage display. Libraries of filamentogenerated which display mutated versions of the lead peptide as a fusion with a phage coat protein.express peptides with high affinity for Mac-1 will be selected from the library by binding to purifiidentified by phage display will be synthesized and assayed in vitro for their ability to inhibit ne