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HS, Hyde JS, Feix JB.Biophysics Research Institute, Medical College of Wisconsin, Milwaukee 53226.The binding and state of aggregation of cecropin in large unilamellar vesicles of different surface potential and varying acyl chain length were examined using a Cys-33 spin-labeled derivative of cecropin AD (CAD). Association isotherms of the peptide were measured for vesicles neutrophil alpha of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylcholine neutrophil alpha (POPC) containing 5, 15, and 30 mol % 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylglycerol (POPG). The isotherms display a concentration-dependent neutrophil alpha positive cooperativity indicating the possible formation of cecropin aggregates in the lipid phase. The critical aqueous concentration for aggregation was dependent on the fraction of POPG, suggesting the involvement of acidic lipids in the formation and stabilization of the putative aggregate.
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