期刊
BIOPHYSICAL JOURNAL
卷 97, 期 7, 页码 1917-1925出版社
CELL PRESS
DOI: 10.1016/j.bpj.2009.05.066
关键词
-
类别
资金
- National Science Foundation [DMR0 117792]
- Nanotoxicology Interdisciplinary Research Team program [CBET 0608978]
- National Institute of General Medical Sciences Biomolecular Science and Engineering training program fellowship
- Rensselaer Polytechnic Institute
Recent molecular-dynamics simulations have suggested that the arginine-rich HIV Tat peptides translocate by destabilizing and inducing transient pores in phospholipid bilayers. In this pathway for peptide translocation, Arg residues play a fundamental role not only in the binding of the peptide to the surface of the membrane, but also in the destabilization and nucleation of transient pores across the bilayer. Here we present a molecular-dynamics simulation of a peptide composed of nine Args (Arg-9) that shows that this peptide follows the same translocation pathway previously found for the Tat peptide. We test experimentally the hypothesis that transient pores open by measuring ionic currents across phospholipid bilayers and cell membranes through the pores induced by Arg-9 peptides. We find that Arg-9 peptides, in the presence of an electrostatic potential gradient, induce ionic currents across planar phospholipid bilayers, as well as in cultured osteosarcoma cells and human smooth muscle cells. Our results suggest that the mechanism of action of Arg-9 peptides involves the creation of transient pores in lipid bilayers and cell membranes.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据