Inhibitory effect of collagen-derived tripeptides on dipeptidylpeptidase-IV activity. (December 2014)

• Record Type: Journal Article
• Authors: Hatanaka, Tadashi; Kawakami, Kayoko; Uraji, Misugi
• Is Part Of: Journal of enzyme inhibition and medicinal chemistry. Volume 29:Number 6(2014:Dec.)
• Page Start: 823
• Page End: 828
• Publication Date: 2014-12
• Subjects: Enzyme inhibitors -- Periodicals; Enzyme Inhibitors -- periodicals; Biochemistry -- periodicals; 572.7
• DOI: 10.3109/14756366.2013.858143
• Languages: English
• ISSNs: 1475-6366

Abstract

<abstract> <title>Abstract</title> <p>The collagen tripeptide fragments Gly-Ala-Hyp, Gly-Pro-Ala and Gly-Pro-Hyp were generated by hydrolyzing collagen from pig-skin, cattle-skin, fish-scales and chicken-feet, respectively, with <italic>Streptomyces</italic> collagenase. Collagenase treatment increased the concentration of tripeptides in the hydrolysates by 13–15% (w/w). Of the three peptides, Gly-Pro-Hyp was a true peptidic inhibitor of dipeptidylpeptidase-IV (DPP-IV), because DPP-IV could not hydrolyze the bond between Pro-Hyp. This tripeptide was a moderately competitive inhibitor (<italic>K</italic>_i = 4.5 mM) of DPP-IV, and its level in the collagen hydrolysates could be greatly increased (4–9% [w/w]) using <italic>Streptomyces</italic> collagenase.</p> </abstract>