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报道了一种从噬菌体肽库中筛选胰凝乳蛋白酶短肽抑制剂的新方法．在通常的亲和富集筛选的基础上，利用胰凝乳蛋白酶自身的水解活力切割掉结合的底物噬菌体，再经抑制活力分析得到抑制性噬菌体克隆．这样筛得的噬菌体克隆具有明显的胰凝乳蛋白酶结合活力和抑制活力，ＤＮＡ序列分析发现其保守序列为（Ｓ／Ｔ）ＲＶＰＲ（Ｒ／Ｈ）．按此序列化学合成的短肽Ａｃ－ＡＳＲＶＰＲＲＧ－ＮＨ２、Ａｃ－ＡＳＲＶＰＲＨＧ－ＮＨ２同样表现出对胰凝乳蛋白酶的抑制作用．该方法为蛋白酶短肽抑制剂的筛选提供了一条有效途径
A new method for screening chymotrypsin short peptide inhibitors from phage peptide libraries was reported. On the basis of usual affinity enrichment screening, the bound phage was cleaved by the hydrolytic activity of chymotrypsin itself, and then the inhibitory phage clones were obtained by the inhibition activity analysis. The phage clones screened in this way showed significant chymotrypsin binding activity and inhibitory activity. The DNA sequence analysis showed that the conserved sequence was (S / T) RVPR (R / H). Ac-ASRVPRRG-NH2, a chemically synthesized short peptide of this sequence, also showed an inhibitory effect on chymotrypsin by Ac-ASRVPRHG-NH2. This method provides an effective way for protease short peptide screening