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  • Inhibitory effect of collagen-derived tripeptides on dipeptidylpeptidase-IV activity.

Inhibitory effect of collagen-derived tripeptides on dipeptidylpeptidase-IV activity.

Journal of enzyme inhibition and medicinal chemistry (2014-03-22)
Tadashi Hatanaka, Kayoko Kawakami, Misugi Uraji
ABSTRACT

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 Streptomyces 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 (Ki=4.5 mM) of DPP-IV, and its level in the collagen hydrolysates could be greatly increased (4-9% [w/w]) using Streptomyces collagenase.

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