4.5 Article

Novel Dipeptidyl Peptidase-4-Inhibiting Peptide Derived From β-Lactoglobulin

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JOURNAL OF PHARMACOLOGICAL SCIENCES
卷 117, 期 1, 页码 63-66

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JAPANESE PHARMACOLOGICAL SOC
DOI: 10.1254/jphs.11089SC

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DPP-4 inhibitor; beta-lactoglobulin; Val-Ala-Gly-Thr-Trp-Tyr

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Trypsin-treated beta-lactoglobulin significantly decreased the glucose level after an oral glucose tolerance test using mice. We performed the present study to identify the active peptide inhibiting dipepticlyl peptidase-4 from trypsin-treated beta-lactoglobulin. Trypsin-treated beta-lactoglobulin showed a concentration-dependent inhibition for dipeptidyl peptidase-4, with an IC(50) value of 210 mu M, although non-treated,beta-lactoglobulin showed no significant effect in the in vitro assay. The active peptide was isolated from trypsin-treated beta-lactoglobulin and identified as the hexapeptide Val-Ala-Gly-Thr-Trp-Tyr (beta-lactoglobulin f15-20). This hexapeptide also exhibited a concentration-dependent inhibitory effect and IC(50) value was 174 mu M, suggesting that this hexapeptide is almost totally responsible for the DPP-4 inhibitory activity of trypsin-treated beta-lactoglobulin.

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