Lambert P, Kuroda H, Chino N, Watanabe T X, Kimura T, Sakakibara S
Peptide Institute Inc., Protein Research Foundation, Osaka, Japan.
Biochem Biophys Res Commun. 1990 Jul 31;170(2):684-90. doi: 10.1016/0006-291x(90)92145-p.
Charybdotoxin, a 37 amino acid peptide which is a minor component of Leiurus quinquestriatus venom, was synthesized by the solution procedure applying our maximum protection strategy. After formation of the three disulfide bonds, for which a redox buffer was necessary, the final product was purified to homogeneity and found to have similar biological potency to that reported by others for the natural product. The disulfide bond configuration was found to be: Cys7-Cys28; Cys13-Cys33; Cys17-Cys35. Conformational analysis by 1H-NMR showed that the molecule exists as a very tightly folded structure, in which residues 1-7 and 24-37 form a triple-stranded beta-sheet, with a turn at positions 30-31. The region from 11-20 appears to adopt an alpha-helical conformation.
芋螺毒素是一种由37个氨基酸组成的肽，是金环蛇毒液的次要成分，采用我们的最大保护策略通过溶液法合成。在形成三个二硫键（为此需要氧化还原缓冲液）后，最终产物被纯化至同质，并发现其生物活性与其他报道的天然产物相似。发现二硫键构型为：Cys7-Cys28；Cys13-Cys33；Cys17-Cys35。通过1H-NMR进行的构象分析表明，该分子以非常紧密折叠的结构存在，其中残基1-7和24-37形成三链β-折叠，在30-31位有一个转角。11-20区域似乎采用α-螺旋构象。
