期刊论文详细信息
Biology
An Integrated Peptidomics and In Silico Approach to Identify Novel Anti-Diabetic Peptides in Parmigiano-Reggiano Cheese
Valentina Pizzamiglio1  Serena Martini2  Lisa Solieri2  Davide Tagliazucchi2  Alice Cattivelli2 
[1]Consorzio del Formaggio Parmigiano Reggiano, 42124 Reggio Emilia, Italy
[2]Department of Life Sciences, University of Modena and Reggio Emilia, 42100 Reggio Emilia, Italy
关键词: bioactive peptides;    type-2-diabetes;    enzyme inhibition;    mass spectrometry;    Parmigiano-Reggiano;    peptidomics;   
DOI  :  10.3390/biology10060563
来源: DOAJ
【 摘 要 】
Inhibition of key metabolic enzymes linked to type-2-diabetes (T2D) by food-derived compounds is a preventive emerging strategy in the management of T2D. Here, the impact of Parmigiano-Reggiano (PR) cheese peptide fractions, at four different ripening times (12, 18, 24, and 30 months), on the enzymatic activity of α-glucosidase, α-amylase, and dipeptidyl peptidase-IV (DPP-IV) as well as on the formation of fluorescent advanced glycation end-products (fAGEs) was assessed. The PR peptide fractions were able to inhibit the selected enzymes and fAGEs formation. The 12-month-ripening PR sample was the most active against the three enzymes and fAGEs. Mass spectrometry analysis enabled the identification of 415 unique peptides, 54.9% of them common to the four PR samples. Forty-nine previously identified bioactive peptides were found, mostly characterized as angiotensin-converting enzyme-inhibitors. The application of an integrated approach that combined peptidomics, in silico analysis, and a structure–activity relationship led to an efficient selection of 6 peptides with potential DPP-IV and α-glucosidase inhibitory activities. Peptide APFPE was identified as a potent novel DPP-IV inhibitor (IC50 = 49.5 ± 0.5 μmol/L). In addition, the well-known anti-hypertensive tripeptide, IPP, was the only one able to inhibit the three digestive enzymes, highlighting its possible new and pivotal role in diabetes management.
【 授权许可】

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