Woolley G A, Wallace B A
Department of Crystallography, Birkbeck College, University of London, U.K.
Biochemistry. 1993 Sep 21;32(37):9819-25. doi: 10.1021/bi00088a037.
The interaction of the voltage-dependent channel-forming peptide alamethicin with dioleoylphosphatidylcholine (DOPC) small unilamellar vesicles (SUV) has been studied using circular dichroism spectroscopy over a range of wavelengths and temperatures. Evidence is presented for the existence of two distinct membrane-bound states of the peptide which reflect different extents of peptide-peptide interaction. An elevated temperature is found to diminish the apparent peptide-peptide interaction. These results provide insight into the general problem of helix-helix interaction in membranes and provide experimental support for the proposal [Popot, J. L., & Engelman, D. M. (1990) Biochemistry 29, 4031-4037] that these interactions can be enthalpically favorable.
利用圆二色光谱在一系列波长和温度范围内研究了电压依赖性通道形成肽阿拉米辛与二油酰磷脂酰胆碱（DOPC）小单层囊泡（SUV）的相互作用。有证据表明该肽存在两种不同的膜结合状态，这反映了肽 - 肽相互作用的不同程度。发现升高温度会减少明显的肽 - 肽相互作用。这些结果为膜中螺旋 - 螺旋相互作用的一般问题提供了见解，并为[波波特，J. L.，& 恩格尔曼，D. M.（1990）《生物化学》29，4031 - 4037]中提出的这些相互作用在焓方面可能有利的观点提供了实验支持。
