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Aminoethyl chitooligosaccharides inhibit the activity of angiotensin converting enzyme

Paper ID Volume ID Publish Year Pages File Format Full-Text
35925 45114 2008 5 PDF Available
Title
Aminoethyl chitooligosaccharides inhibit the activity of angiotensin converting enzyme
Abstract

In the present research, chitooligosaccharides (COS) with molecular weight 800–3000 Da and 90% of deacetylation were chemically modified by grafting 2-chloroethylamino hydrochloride at C-6 position to synthesize angiotensin I converting enzyme (ACE) inhibitory chitin derivatives based on the properties of ACE inhibitors. The synthetic product was designated as aminoethyl chitooligosaccharide (AE-COS) with molecular weight 800.79–4765 Da. Its IC50 value on ACE was 0.8017 μg/mL. Furthermore, Lineweaver-Burk plots revealed that the inhibition was competitive via obligatory binding site of ACE. Therefore, these results exhibited that substitution of the hydrogen atom at the C-6 position of pyranose residue by the aminoethyl group promotes ACE inhibitory effects of COS.

Keywords
Chitooligosaccharides (COS); Aminoethyl COS; Competitive inhibitor; Angiotensin I converting enzyme (ACE); Chitosan; Chitin
First Page Preview
Aminoethyl chitooligosaccharides inhibit the activity of angiotensin converting enzyme
Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 43, Issue 1, January 2008, Pages 119–123
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering