A study to evaluate the potential of an in silico approach for predicting dipeptidyl peptidase-IV inhibitory activity in vitro of protein hydrolysates

• Published in: Food chemistry 2017-11, Vol.234, p.431-438
• Main Authors: Wang, Tzu-Yuan, Hsieh, Cheng-Hong, Hung, Chuan-Chuan, Jao, Chia-Ling, Lin, Pei-Yi, Hsieh, You-Liang, Hsu, Kuo-Chiang
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Computer Simulation; Correlation analysis; Dietary protein; Dipeptidyl Peptidase 4 - metabolism; Dipeptidyl peptidase IV inhibitor; Dipeptidyl-Peptidase IV Inhibitors - pharmacology; In silico analysis; Protein Hydrolysates - metabolism
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2017.05.035

•The in silico parameter, frequency (A), was applied as a screening tool.•294 proteins and 5 proteases listed in the BIOPEP database were analyzed in silico.•Numbers of peptides with Xaa-Pro and Xaa-Ala was the key factor of frequency.•Frequency and DPP-IV inhibitory activity in vitro showed a strong correlation. A total of 294 edible protein sequences and 5 commercial proteases listed in the BIOPEP database were analyzed in silico. The frequency (A), a parameter in silico described previously, was examined further to calculating the ratio of truncated peptides with Xaa-proline and/or Xaa-alanine to all peptide fragments in a protein hydrolyzed with a protease, using the BIOPEP database. Then the in vitro DPP-IV inhibitory activity was determined using the same 15 protein and protease combinations to evaluate their relationship. The result shows that A values considering the number of Xaa-proline+Xaa-alanine exhibited a strong correlation with in vitro DPP-IV inhibition rates by Pearson’s correlation analysis (r=0.6993; P