Keire D A, Fletcher T G
Beckman Research Institute of the City of Hope, California 91010-0269, USA.
Biophys J. 1996 Apr;70(4):1716-27. doi: 10.1016/S0006-3495(96)79734-5.
NMR and CD studies have been used to analyze the model membrane-bound structure of the neuropeptide substance P (RPKPQQFFGLM-NH2, SP), which has previously been proposed as the NK1 receptor active form. Conformations were determined for the SP in the presence of aqueous solutions of zwitterionic dodecylphosphocholine (DPC) and anionic sodium dodecylsulfate (SDS) micelles. The two structures are similar, although fast exchange between free and bound forms was observed for SP with DPC micelles, and predominantly bound characteristics were found for SP in SDS. The addition of 150-200 mM NaCl had no observable effect on the bound conformation in either case. Thus, the structure of SP at a micelle surface is determined largely by hydrophobic forces, and the electrostatic interactions determine the amount of SP that is bound.
核磁共振(NMR)和圆二色(CD)研究已被用于分析神经肽P物质(RPKPQQFFGLM-NH2,SP)的模型膜结合结构,该神经肽先前被认为是NK1受体的活性形式。在两性离子十二烷基磷酸胆碱(DPC)和阴离子十二烷基硫酸钠(SDS)胶束的水溶液存在下,测定了SP的构象。两种结构相似,尽管观察到SP与DPC胶束之间存在游离形式和结合形式的快速交换,并且在SDS中发现SP主要具有结合特性。在这两种情况下,添加150 - 200 mM NaCl对结合构象均无明显影响。因此,SP在胶束表面的结构在很大程度上由疏水力决定,而静电相互作用决定了结合的SP的量。