Erne D, Sargent D F, Schwyzer R
Biochemistry. 1985 Jul 30;24(16):4261-3. doi: 10.1021/bi00337a001.
Infrared attenuated total reflection (IR-ATR) spectroscopy and capacitance minimization (CM) were used to study the secondary structure, orientation, and accumulation of dynorphin A-(1-13)-tridecapeptide (dynorphin1-13) molecules on the surface of planar membranes prepared from 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine. The peptide assumed a helical structure oriented perpendicularly on the membrane surface. Binding from aqueous solutions containing 10 mM KCl saturated reversibly at about a bilayer area of 110 nm2 per peptide molecule, an apparent dissociation constant of 11 microM, and rate constants of 2 X 10(2) s-1 (adsorption) and 2 X 10(-3) s-1 (desorption). The results complement those obtained by vesicle-mediated hydrophobic labeling [Gysin, B., & Schwyzer, R. (1983) Arch. Biochem. Biophys. 225, 467-474]. They indicate that the behavior of this amphiphilic peptide in contact with neutral lipid membranes may be quite different from that in molecularly disperse or micellar solutions of detergents or lysolecithins and that, in the case of dynorphin1-13, primary amphiphilicity overrules secondary amphiphilicity.
采用红外衰减全反射（IR - ATR）光谱法和电容最小化（CM）技术，研究了强啡肽A -（1 - 13）-十三肽（强啡肽1 - 13）分子在由1 - 棕榈酰 - 2 - 油酰 - sn - 甘油 - 3 - 磷酸胆碱制备的平面膜表面的二级结构、取向和聚集情况。该肽呈现出垂直于膜表面取向的螺旋结构。在含有10 mM KCl的水溶液中，每肽分子在约110 nm²的双层面积处可逆饱和结合，表观解离常数为11 μM，吸附速率常数为2×10² s⁻¹，解吸速率常数为2×10⁻³ s⁻¹。这些结果补充了通过囊泡介导的疏水标记法获得的结果[吉辛，B.，& 施维泽，R.（1983年）《生物化学与生物物理学文献》225，467 - 474]。它们表明，这种两亲性肽与中性脂质膜接触时的行为可能与在洗涤剂或溶血卵磷脂的分子分散或胶束溶液中的行为有很大不同，并且就强啡肽1 - 13而言，一级两亲性优先于二级两亲性。
