期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 127, 期 42, 页码 9095-9101出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.3c05385
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In this study, the spontaneous binding of PAP248-286 fusogenic peptide to membrane bilayers was investigated using coarse-grained molecular dynamics simulations. The simulations revealed that PAP248-286 displayed increased binding to the membrane in the presence of anionic lipid POPG, particularly in systems containing charged histidine (His) residues. The peptide adopted a parallel orientation with the membrane, exposing its positively charged residues to the lipid bilayer. These findings provide insights into the molecular mechanisms underlying the membrane binding of PAP248-286 and its potential role in HIV fusion and infection.
PAP248-286 is a fusogenic peptide derived from prostatic acid phosphatase, commonly found in human semen, and is known to mediate HIV fusion with cell membranes. In this study, we performed 120 independent coarse-grained molecular dynamics simulations to investigate the spontaneous binding of PAP248-286 monomers, considering both charged and neutral histidine (His) residues, to membrane bilayers composed of different lipid compositions: 100% POPC, 70% POPC-30% POPG, and 50% POPC-50% POPG. Our simulations revealed that PAP248-286 displayed spontaneous binding to the membrane, with increased binding observed in the presence of anionic lipid POPG. Specifically, in systems containing 30% and 50% POPG lipids, monomer residues, particularly in the systems containing charged histidine (His) residues, exhibited prolonged binding with the membrane. Furthermore, our simulations indicated that PAP248-286 adopted a parallel orientation with the membrane, exposing its positively charged residues to the lipid bilayer. Interestingly, systems containing charged His residues showed a higher lipid occupancy around the peptide. These findings are consistent with previous experimental data, suggesting that PAP248-286 binding is enhanced in membranes with charged His residues, resembling the conditions found in the acidic vaginal pH environment. The results of our study provide further insights into the molecular mechanisms underlying the membrane binding of PAP248-286, contributing to our understanding of its potential role in HIV fusion and infection.
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