SEQUENTIAL HYDROPHOBIC POLYPEPTIDES CONSISTING OF LEUCINE AND ISOLEUCINE - SYNTHESIS, CONFORMATIONAL CHARACTERIZATION IN THE SOLID-STATE, AND GOVERNING FACTORS FOR THE SPECIFICATION IN THE BETA-STRUCTURE ALPHA-HELIX DECISION

被引：5

作者：

KOBAYASHI, K ^{[1
]}

YONEZAWA, N ^{[1
]}

KATAKAI, R ^{[1
]}

机构：

[1] GUNMA UNIV,FAC ENGN,DEPT CHEM,KIRYU,GUMMA 376,JAPAN

来源：

MACROMOLECULES | 1995年 / 28卷 / 24期

关键词：

D O I：

10.1021/ma00128a038

中图分类号：

O63 [高分子化学（高聚物）];

学科分类号：

070305 ; 080501 ; 081704 ;

摘要：

Six new sequential hydrophobic polypeptides consisting of leucyl and isoleucyl residues were synthesized by polycondensation of peptide active esters. Solid samples of these polypeptides were obtained by fast reprecipitation from a solution in 1,1,1,3,3,3-hexafluoropropan-2-ol (HFIP) or HFIP/dichloroacetic acid with diethyl ether. The conformation of the solid sample was determined by IR spectroscopy as follows: the beta-structure for (Leu-Ile-Ile-Leu)(n), a mixture of the beta-structure and alpha-helix for (Leu-Ile-Leu)(n), and the alpha-helix for (Ala-Ile-Ile-Leu)(n), (D-Leu-Ile-Ile-Leu)(n), (Leu-Ile-Ile-Gly)(n), and (Leu-Ile-Ile-Aib)(n). The factor governing the specification of the beta-structure/alpha-helix was deduced to be the consecutiveness of the tidily aligned hydrophobic side chains of the amino acid residues to afford sterically well-regulated intermolecular aggregation of the polypeptides prior to the conformational preference of the individual amino acid residue.

引用

页码：8242 / 8246

页数：5

共 25 条

[1] THE STRUCTURE OF SYNTHETIC POLYPEPTIDES .2. INVESTIGATION WITH POLARIZED INFRA-RED SPECTROSCOPY [J].