Department of Chemistry, City College of New York/CUNY, New York, NY 10031, USA.
Biophys Chem. 2012 Feb;161(1):1-7. doi: 10.1016/j.bpc.2011.10.002. Epub 2011 Oct 30.
The implicit membrane model IMM1 is extended to include the membrane dipole potential and applied to molecular dynamics simulations of the helical peptides alamethicin, WALP23, influenza hemagglutinin fusion peptide, HIV fusion peptide, magainin, and the pre-sequence of cytochrome c oxidase subunit IV (p25). The results show that the orientation of the peptides in the membrane can be influenced by the dipole potential. The binding affinity of all peptides except for the hemagglutinin fusion peptide decreases upon increase of the dipole potential. The changes in both orientation and binding affinity are explained by the interaction of the dipole potential with the helix backbone dipole and ionic side-chains. In general, peptides that tend to insert the N-terminus in the membrane and/or have positively charged side chains will lose binding affinity upon increase of the dipole potential.
将包含膜偶极势的隐式膜模型 IMM1 进行扩展，并将其应用于螺旋肽 alamethicin、WALP23、流感血凝素融合肽、HIV 融合肽、magainin 和细胞色素 c 氧化酶亚基 IV（p25）前序列的分子动力学模拟。结果表明，膜偶极势可以影响肽的取向。除了血凝素融合肽外，所有肽的结合亲和力都会随着偶极势的增加而降低。偶极势与螺旋主链偶极和离子侧链的相互作用可以解释取向和结合亲和力的变化。一般来说，倾向于将 N 端插入膜内且/或具有正电荷侧链的肽在偶极势增加时会失去结合亲和力。
