原创力文档sdpi, the first functionally characterized kunitz-type trypsin inhibitor from scorpion venomsdpi,第一个功能特征kunitz-type蝎毒的胰蛋白酶抑制剂.pdfVIP
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sdpi, the first functionally characterized kunitz-type trypsin inhibitor from scorpion venomsdpi,第一个功能特征kunitz-type蝎毒的胰蛋白酶抑制剂
SdPI, The First Functionally Characterized Kunitz-Type
Trypsin Inhibitor from Scorpion Venom
. . .
Ruiming Zhao , Hui Dai , Su Qiu , Tian Li, Yawen He, Yibao Ma, Zongyun Chen, Yingliang Wu, Wenxin
Li*, Zhijian Cao*
State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, People’s Republic of China
Abstract
Background: Kunitz-type venom peptides have been isolated from a wide variety of venomous animals. They usually have
protease inhibitory activity or potassium channel blocking activity, which by virtue of the effects on predator animals are
essential for the survival of venomous animals. However, no Kunitz-type peptides from scorpion venom have been
functionally characterized.
Principal Findings: A new Kunitz-type venom peptide gene precursor, SdPI, was cloned and characterized from a venom
gland cDNA library of the scorpion Lychas mucronatus. It codes for a signal peptide of 21 residues and a mature peptide of
59 residues. The mature SdPI peptide possesses a unique cysteine framework reticulated by three disulfide bridges, different
from all reported Kunitz-type proteins. The recombinant SdPI peptide was functionally expressed. It showed trypsin
inhibitory activity with high potency (Ki = 1.6 61027 M) and thermostability.
Conclusions: The results illustrated that SdPI is a potent and stable serine protease inhibitor. Further mutagenesis and
molecular dynamics simulation revealed that SdPI possesses a serine protease inhibitory active site similar to other Kunitz-
type venom peptides. To our knowledge, SdPI is the first functionally characterized Kunitz-type trypsin inhibitor derived
from scorpion venom, and it represents a new class of Kunitz-type venom peptides.
Citation: Zhao R, Dai
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