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Extraction of tripeptide-inhibitor angiotensin converting enzyme (Ile-Gln-Pro) from spirulina and investigate the relationship between the structure and activity of ACE inhibitor tripeptides use of BIOPEP database

Document Type : Article

Authors

1 Department of Biochemistry,Faculty of Basic Sciences,ttPayame Noor University.Isfahan,Iran

2 Professor, Isfahan Payam-e Noor University, Isfahan, Iran

3 Associate Professor, Isfahan Payam-e Noor University, Isfahan, Iran

4 ssociate Professor, Isfahan Payam-e Noor University, Isfahan, Iran

Abstract

Abstract
High blood pressure doubles the risk of cardiovascular disease. In addition to chemical drugs, biodegradable peptides have antihypertensive properties and the Ile-Gln-Pro peptide is one of these peptides. Spirulina is a green-blue algae of the cyanobacteria branch, which is now used as a supplement to the pharmaceutical industry. The Ile-Gln-Pro peptide was extracted from Spirulina platensis algae using an alkalase enzyme and was analyzed by filtration gel chromatography and RP-HPLC and its inhibitory effect on the ACE enzyme was investigated. ACE enzyme was inhibited by Ile-Gln-Pro peptide by non-competitive inhibition method with Ki = 5.8 μM and IC50 = 0.65 μM . According to the available information from the ACE inhibitor peptide in the BIOPEP database, a comparative study was performed on the location of amino acids in the ACE inhibitor peptide and its effect on the potency of tri-peptide inhibition. Based on SPSS software, on the 196 ACE inhibitor peptide, the presence of Lys, Gly, Thr and Pro amino acids at the end of C and His, Ala, and Met amino acids at the end of N, as well as Phe, Ala, His And His in the middle of peptide have relationship with EC50 and peptide-inhibiting potency.

Keywords

References
 
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Experimental animal Biology
Volume 8, Issue 1 - Serial Number 29
No.1
August 2019
Pages 39-50
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