Bioactivity of collagen peptides derived from commercial animals: In silico investigation

Abstract

Collagen peptides (CP) obtained from collagen hydrolysis have drawn much attention for their broad bioactivities, such as antioxidant, anti-inflammatory, angiotensin-converting enzyme (ACE) and dipeptidyl peptidase-IV (DPP-IV) inhibitory activities. This study employed an in silico approach to investigate the bioactivities of CP from fish, chicken, cattle, pig, yak, sheep, and donkey. BLAST analysis of amino acid sequences showed CP from mammals had comparable bioactivities but those from fish and chicken possessed different bioactivity potential due to low protein homology. In silico hydrolysis of collagen with gastrointestinal enzymes, including trypsin, pepsin, and proteinase K showed that the number of bioactive CP from chicken (922) and mammals (737–905) was higher than that from fish (544–675) because of the lower content of proline in fish collagen, but the amount of bioactive peptides percentage to the total peptides generated for tilapia was the highest (86.4%). The most common bioactivities were ACE and DPP-IV inhibitory activities. A molecular docking study showed that Thr-Phe and Gly-Phe had the strongest binding energy to enzymes involved in ACE and DPP-IV, respectively, indicating that collagen was a good source of anti-hypotensive and anti-hypoglycaemic peptides.