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• W2108637812 abstract "Prolyl-rich peptides derived from hydrolysates of bovine caseins have been previously shown to inhibit angiotensin converting enzyme (ACE) activity, suggesting that they may also be able to inhibit the enzymatic activities of prolyl-specific peptidases. This study shows that peptides derived from αS1-casein and β-casein inhibited the enzymatic activities of purified recombinant matrix metalloprotease (MMP)-2, MMP-7, and MMP-9. The inhibitory efficacy was sequence-dependent. These peptides also selectively inhibited the enzymatic activities of prolyl-amino-peptidases, prolyl-amino-dipeptidases, and prolyl-endopeptidases in extracts of HT-29 and SW480 human colon carcinoma cells, but not in intact cells. They were not cytotoxic or growth inhibitory for these cells. Thus, the prolyl-rich selected peptides were good and selective inhibitors of MMPs and post-proline-cleaving proteases, demonstrating their potential to control inadequate proteolytic activity in the human digestive tract, without inducing cytotoxic effects." @default.
• W2108637812 created "2016-06-24" @default.
• W2108637812 creator A5039449677 @default.
• W2108637812 creator A5069326307 @default.
• W2108637812 creator A5087387177 @default.
• W2108637812 date "2010-12-02" @default.
• W2108637812 modified "2023-10-17" @default.
• W2108637812 title "Peptides from Lactobacillus Hydrolysates of Bovine Milk Caseins Inhibit Prolyl-peptidases of Human Colon Cells" @default.
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• W2108637812 doi "https://doi.org/10.1021/jf102803a" @default.
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