Small peptides derived from the Lys active fragment of the mung bean trypsin inhibitor are fully active against trypsin
文献类型:期刊论文
作者 | Qi, RF; Liu, ZX; Xu, SQ; Zhang, L; Shao, XX; Chi, CW |
刊名 | FEBS JOURNAL |
出版日期 | 2010 |
卷号 | 277期号:1页码:224-232 |
关键词 | Bowman-Birk inhibitor (BBI) gene cloning gene expression inhibitory activity peptide synthesis |
通讯作者 | Chi, CW (reprint author), Chinese Acad Sci, Shanghai Inst Biochem & Cell Biol, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.,zwqi@sibs.ac.cn |
英文摘要 | 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. |
学科主题 | Biochemistry & Molecular Biology |
类目[WOS] | Biochemistry & Molecular Biology |
关键词[WOS] | AMINO-ACID-SEQUENCE ; BOWMAN-BIRK INHIBITOR ; PHASEOLUS AUREUS ROXB ; PROTEASE INHIBITORS ; SEEDS ; CONCENTRATE ; GERMINATION ; COMPLEX ; PLANTS ; FORMS |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000272836100022 |
版本 | 出版稿 |
源URL | [http://202.127.25.143/handle/331003/932] |
专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
推荐引用方式 GB/T 7714 | Qi, RF,Liu, ZX,Xu, SQ,et al. Small peptides derived from the Lys active fragment of the mung bean trypsin inhibitor are fully active against trypsin[J]. FEBS JOURNAL,2010,277(1):224-232. |
APA | Qi, RF,Liu, ZX,Xu, SQ,Zhang, L,Shao, XX,&Chi, CW.(2010).Small peptides derived from the Lys active fragment of the mung bean trypsin inhibitor are fully active against trypsin.FEBS JOURNAL,277(1),224-232. |
MLA | Qi, RF,et al."Small peptides derived from the Lys active fragment of the mung bean trypsin inhibitor are fully active against trypsin".FEBS JOURNAL 277.1(2010):224-232. |
入库方式: OAI收割
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