Identification and molecular docking of tyrosinase inhibitory peptides from allophycocyanin in Spirulina platensis.

This experiment shows that DER can effectively inhibit tyrosinase activity. His244, His259, His260, and Asn260 are the critical residues that drive the interaction between the peptide and tyrosinase, and hydrogen bonding is an important force. DER from Spirulina has the potential to develop functional products with tyrosinase inhibition. This article is protected by copyright. All rights reserved.