Forood B, Pérez-Payá E, Houghten R A, Blondelle S E
Torrey Pines Institute for Molecular Studies, San Diego, California, USA.
Biochem Biophys Res Commun. 1995 Jun 6;211(1):7-13. doi: 10.1006/bbrc.1995.1770.
We have designed a 16-mer peptide composed of a stretch of alanine residues (Ac-KA14K-NH2) which is an effective, simple model for the study of beta-sheet formation in the hydrophobic cores of proteins. This peptide adopts an aqueous soluble "bundling" macromolecular beta-sheet structure, which is extremely stable to a wide range of pHs, temperatures and/or denaturants. Its unusual stability appears to be due to tight hydrophobic packing of the alanine residues in multilayer sheets or micellar forms with the multimeric lysine array being directed outward at the aqueous environment, allowing aqueous solubility.
我们设计了一种由一段丙氨酸残基组成的16聚体肽（Ac-KA14K-NH2），它是研究蛋白质疏水核心中β-折叠形成的有效且简单的模型。这种肽采用水溶性的“聚集”大分子β-折叠结构，对广泛的pH值、温度和/或变性剂具有极高的稳定性。其不同寻常的稳定性似乎是由于丙氨酸残基在多层片层或胶束形式中紧密的疏水堆积，多聚赖氨酸阵列在水环境中向外定向，从而实现水溶性。
