Trypsin inhibitory loop is an excellent lead structure to design serine protease inhibitors and antimicrobial peptides

	Trypsin inhibitory loop is an excellent lead structure to design serine protease inhibitors and antimicrobial peptides
	Li JX 1,6; Zhang C 2,5; Xu XQ 1,6; Wang J 2,5; Yu HN 4; Lai R[]1; Gong WM[]2; rlai@mail.kiz.ac.cn ; wgong@ibp.ac.cn
	2007
发表期刊	FASEB JOURNAL
ISSN	0892-6638
卷号	21 期号:10 页码:2466-2473
合作性质	其它
摘要	The disulfide-bridged hendecapeptide (CWTKSIPPKPC) loop, derived from an amphibian skin peptide, is found to have strong trypsin inhibitory capability. This loop, called the trypsin inhibitory loop (TIL), appears to be the smallest serine protease inhibitor known. A series of synthetic peptides derived from this loop also exhibits trypsin inhibitory activity; some peptides even exhibit both antimicrobial and trypsin inhibitory activities. Antimicrobial peptides are attractive candidates for producing novel antibiotics, but their sensitivity to trypsin-like proteases appreciably limits their application. Bifunctional peptides with both antimicrobial and trypsin inhibitory activities could be ideal candidates for clinical antibiotics, since these reported synthetic peptides have shown resistance against trypsin. The crystal structure of a complex of trypsin with one TIL derivative is solved. The concept of TIL is introduced in this paper. Novel trypsin inhibitors or antimicrobial peptides can be designed readily on the basis of the TIL. Furthermore, functional analysis and a precursor comparison suggest that serine protease inhibitors may have a common ancestor with antimicrobial peptides.
关键词	Trypsin Resistance
资助者	This work was supported by the Chinese National Natural Science Foundation (30570360, 30670456), Yunnan Natural Science Foundation (2005C0054M), and Jiangsu Natural Science Foundation (BK2005422). ; This work was supported by the Chinese National Natural Science Foundation (30570360, 30670456), Yunnan Natural Science Foundation (2005C0054M), and Jiangsu Natural Science Foundation (BK2005422). ; This work was supported by the Chinese National Natural Science Foundation (30570360, 30670456), Yunnan Natural Science Foundation (2005C0054M), and Jiangsu Natural Science Foundation (BK2005422). ; This work was supported by the Chinese National Natural Science Foundation (30570360, 30670456), Yunnan Natural Science Foundation (2005C0054M), and Jiangsu Natural Science Foundation (BK2005422).
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收录类别	SCI
语种	英语
资助者	This work was supported by the Chinese National Natural Science Foundation (30570360, 30670456), Yunnan Natural Science Foundation (2005C0054M), and Jiangsu Natural Science Foundation (BK2005422). ; This work was supported by the Chinese National Natural Science Foundation (30570360, 30670456), Yunnan Natural Science Foundation (2005C0054M), and Jiangsu Natural Science Foundation (BK2005422). ; This work was supported by the Chinese National Natural Science Foundation (30570360, 30670456), Yunnan Natural Science Foundation (2005C0054M), and Jiangsu Natural Science Foundation (BK2005422). ; This work was supported by the Chinese National Natural Science Foundation (30570360, 30670456), Yunnan Natural Science Foundation (2005C0054M), and Jiangsu Natural Science Foundation (BK2005422).
文献类型	期刊论文
条目标识符	http://ir.kiz.ac.cn/handle/152453/2509
专题	科研部门_天然药物功能蛋白质学科组（赖仞）科研部门_动物模型与人类重大疾病机理重点实验室
通讯作者	rlai@mail.kiz.ac.cn; wgong@ibp.ac.cn
作者单位	1.Biotoxin Units of Key Laboratory of Animal Models and Human Disease Mechanisms, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, Yunnan, China 2.Institute of Biophysics, Chinese Academy of Sciences, Beijing, China 3.Key Laboratory of Microbiological Engineering of Agricultural Environment, Ministry of Agriculture, Life Sciences College of Nanjing Agricultural University, Nanjing, Jiangsu, China 4.College of Life Sciences of Heibei Normal University, Shijiazhuang, Hebei, China 5.School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, China 6.Graduate School of the Chinese Academy of Sciences, Beijing, China
推荐引用方式 GB/T 7714	Li JX,Zhang C,Xu XQ,et al. Trypsin inhibitory loop is an excellent lead structure to design serine protease inhibitors and antimicrobial peptides[J]. FASEB JOURNAL,2007,21(10):2466-2473.
APA	Li JX.,Zhang C.,Xu XQ.,Wang J.,Yu HN.,...&wgong@ibp.ac.cn.(2007).Trypsin inhibitory loop is an excellent lead structure to design serine protease inhibitors and antimicrobial peptides.FASEB JOURNAL,21(10),2466-2473.
MLA	Li JX,et al."Trypsin inhibitory loop is an excellent lead structure to design serine protease inhibitors and antimicrobial peptides".FASEB JOURNAL 21.10(2007):2466-2473.

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