Screening of novel bovine elastin derived peptides with elastase inhibition and photoprotective potential: A combined in silico and in vitro study

Background

The demand for food‐based anti‐photoaging products is in a surge because of the rising recognition of health and beauty as well as enhanced comprehension of the detrimental impact of UV radiation. This study aimed to investigate the potential of bioactive peptides derived from bovine elastin, specifically focusing on identifying novel elastase inhibitory peptides and assessing their photoprotective properties using bioinformatics techniques.

Results

A total of 48 bioactive peptides were screened in bovine elastin hydrolysate (EH) utilizing Peptide Ranker analysis. Three novel elastase inhibitory peptides GAGQPFPI, FFPGAG and FPGIG (in descending order of activity) exhibited potent inhibitory effects on elastase in vitro, surpassing the inhibitory effect of EH by a factor of 1‐2 and reaching significantly lower concentrations (8‐15 times lower) as EH. The cumulative inhibitory effect of GAGQPFPI, FFPGAG and FPGIG reached 91.5%. Further analysis revealed that FFPGAG and FPGIG exhibited mixed inhibition, while GAGQPFPI displayed non‐competitive inhibition. Molecular simulations showed that these peptides interacted effectively with the elastase active site through hydrogen bonding and hydrophobic interactions. Furthermore, GAGQPFPI, FFPGAG and FPGIG demonstrated high stability in gastrointestinal digestion, demonstrated transcellular permeability across Caco‐2 cell monolayers, and exhibited remarkable photoprotective properties against UVB‐irradiated HaCaT cells.

Conclusion

GAGQPFPI showed the most promising potential as a functional food with photoprotective effects against UVB damage and inhibitory properties against elastase.

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