Small peptides derived from the Lys active fragment of the mung bean trypsin inhibitor are fully active against trypsin

	Small peptides derived from the Lys active fragment of the mung bean trypsin inhibitor are fully active against trypsin
	Qi, RF; Liu, ZX; Xu, SQ; Zhang, L; Shao, XX; Chi, CW
刊名	FEBS JOURNAL
	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
内容类型	期刊论文
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.