Expression and purification recombinant antihypertensive peptide ameliorates hypertension in rats with spontaneous hypertension.

Abstract:

:A highly efficient Escherichia coli expression system was established to obtain an appreciable quantity of antihypertensive peptide. The DNA-coding sequence for the Gly-Val-Tyr-Pro-His-Lys peptide was chemically synthesized and linked to form a ten-copy in tandem. It was cloned into the vector pET-15b and expressed in E. coli BL21 (DE3). The optimal conditions for maximal expression were verified and included the induction time and the concentration of isopropyl-β-D-thiogalactopyranoside. The recombinant protein was purified by affinity chromatography to greater than 95% purity, and further purification was achieved by High-performance Liquid Chromatography after cleavage with trypsin. The product was identified by Electrospray Ionization-Mass Spectrometry. The antihypertensive effects of the recombinant AHP were investigated in spontaneously hypertensive rats. The in vivo results demonstrated that a single oral administration of this peptide in spontaneously hypertensive rats resulted in a significant reduction of systolic blood pressure at 2h. Systolic blood pressure was stabilized 4h later and remained at a low level for 24h. This study provides a practical method to develop the peptide into functional foods or drugs for the prevention and treatment of hypertension.

journal_name

Protein Expr Purif

authors

Wang XL,Ma SN,Yuan YH,Ding Y,Li DS

doi

10.1016/j.pep.2015.05.001

subject

Has Abstract

pub_date

2015-09-01 00:00:00

pages

30-4

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(15)00101-1

journal_volume

113

pub_type

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