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首页> 外文期刊>The FEBS journal >Small peptides derived from the Lys active fragment of the mung bean trypsin inhibitor are fully active against trypsin
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Small peptides derived from the Lys active fragment of the mung bean trypsin inhibitor are fully active against trypsin

机译：源自绿豆胰蛋白酶抑制剂Lys活性片段的小肽对胰蛋白酶具有完全活性

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摘要

The Bowman-Birk protease inhibitors have recently attracted attention for their potential as cancer preventive and suppressing agents. They contain two canonical binding loops, both consisting of nine highly conserved residues capable of inhibiting corresponding serine proteases. In this study, we cloned the cDNA of the mung bean trypsin inhibitor, one of the most studied Bowman-Birk protease inhibitors. A modified peptide, Lys33GP, with 33 residues derived from the long chain of the Lys active fragment of mung bean trypsin inhibitor, was successfully expressed in Escherichia coli as a glutathione-S-transferase fusion protein. The recombinant product was obtained with a high yield, and exhibited potent inhibitory activity. Meanwhile, a shorter peptide composed of only 16 residues (the Lys16 peptide), corresponding to the active core of the fragment, was synthesized. Both the recombinant and the synthesized peptides had the same inhibitory activity toward trypsin at a molar ratio of 1 : 1, implying that the Lys16 peptide with two disulfide bonds is possibly the essential structural unit for inhibitory activity. Using site-directed mutagenesis, the P-1 position Lys was replaced by Phe, and the resulting mutant, Lys33K/F, was determined to have potent chymotrypsin inhibitory activity. Both Lys33GP and the Lys33K/F mutant may be potential pharmaceutical agents for the prevention of oncogenesis.
机译：Bowman-Birk蛋白酶抑制剂作为癌症预防和抑制剂的潜力最近引起了人们的关注。它们包含两个典型的结合环，均由能够抑制相应丝氨酸蛋白酶的九个高度保守的残基组成。在这项研究中，我们克隆了绿豆胰蛋白酶抑制剂的cDNA，这是研究最多的Bowman-Birk蛋白酶抑制剂之一。一种修饰的肽，Lys33GP，具有来自绿豆胰蛋白酶抑制剂Lys活性片段的长链的33个残基，已作为谷胱甘肽-S-转移酶融合蛋白成功在大肠杆菌中表达。以高产率获得重组产物，并表现出有效的抑制活性。同时，合成了仅由16个残基组成的较短肽（Lys16肽），其对应于该片段的活性核心。重组肽和合成肽均以1：1的摩尔比对胰蛋白酶具有相同的抑制活性，这表明具有两个二硫键的Lys16肽可能是抑制活性的必要结构单元。使用定点诱变，P-1位置的Lys被Phe取代，所得突变体Lys33K / F被确定具有有效的胰凝乳蛋白酶抑制活性。 Lys33GP和Lys33K / F突变体都可能是预防肿瘤发生的潜在药物。

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