Teno N, Tsuboi S, Itoh N, Okamoto H, Okada Y
Biochem Biophys Res Commun. 1987 Mar 13;143(2):749-52. doi: 10.1016/0006-291x(87)91417-3.
The first studies on a series of the small synthetic thiol proteinase inhibitors, conservative common sequences in several thiol proteinase inhibitors, are described. Among the many interesting findings with synthetic thiol proteinase inhibitors was the observation that the most effective analogue, Z-Gln-Val-Val-Ala-Gly-OMe, whose amino and carboxyl groups were protected with Z and OMe, respectively, showed inhibitory activity on papain and cathepsin B and protected papain from egg cystatin, human low-molecular-weight kininogen and T-kininogen-induced inhibition but not from leupeptin-induced inhibition. Moreover, it was revealed that Z-Gln-Val-Val-OMe was the smallest peptide to exhibit a protective effect on papain.
本文描述了对一系列小型合成硫醇蛋白酶抑制剂的首次研究，这些抑制剂在几种硫醇蛋白酶抑制剂中具有保守的共同序列。在合成硫醇蛋白酶抑制剂的众多有趣发现中，观察到最有效的类似物Z-Gln-Val-Val-Ala-Gly-OMe，其氨基和羧基分别用Z和OMe保护，对木瓜蛋白酶和组织蛋白酶B具有抑制活性，并能保护木瓜蛋白酶免受卵半胱氨酸蛋白酶抑制剂、人低分子量激肽原和T-激肽原诱导的抑制，但不能免受亮抑酶肽诱导的抑制。此外，还发现Z-Gln-Val-Val-OMe是对木瓜蛋白酶具有保护作用的最小肽。
