In Silico Identification and Molecular Mechanism of Novel Tyrosinase Inhibitory Peptides Derived from Nacre of <i>Pinctada martensii</i>
Fei Li,
Haisheng Lin,
Xiaoming Qin,
Jialong Gao,
Zhongqin Chen,
Wenhong Cao,
Huina Zheng,
Shaohe Xie
Affiliations
Fei Li
College of Food Science and Technology, National Research and Development Branch Center for Shellfish Processing (Zhanjiang), Guangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, Guangdong Provincial Engineering Technology Research Center of Seafood, Guangdong Province Engineering Laboratory for Marine Biological Products, Guangdong Ocean University, Zhanjiang 524088, China
Haisheng Lin
College of Food Science and Technology, National Research and Development Branch Center for Shellfish Processing (Zhanjiang), Guangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, Guangdong Provincial Engineering Technology Research Center of Seafood, Guangdong Province Engineering Laboratory for Marine Biological Products, Guangdong Ocean University, Zhanjiang 524088, China
Xiaoming Qin
College of Food Science and Technology, National Research and Development Branch Center for Shellfish Processing (Zhanjiang), Guangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, Guangdong Provincial Engineering Technology Research Center of Seafood, Guangdong Province Engineering Laboratory for Marine Biological Products, Guangdong Ocean University, Zhanjiang 524088, China
Jialong Gao
College of Food Science and Technology, National Research and Development Branch Center for Shellfish Processing (Zhanjiang), Guangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, Guangdong Provincial Engineering Technology Research Center of Seafood, Guangdong Province Engineering Laboratory for Marine Biological Products, Guangdong Ocean University, Zhanjiang 524088, China
Zhongqin Chen
College of Food Science and Technology, National Research and Development Branch Center for Shellfish Processing (Zhanjiang), Guangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, Guangdong Provincial Engineering Technology Research Center of Seafood, Guangdong Province Engineering Laboratory for Marine Biological Products, Guangdong Ocean University, Zhanjiang 524088, China
Wenhong Cao
College of Food Science and Technology, National Research and Development Branch Center for Shellfish Processing (Zhanjiang), Guangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, Guangdong Provincial Engineering Technology Research Center of Seafood, Guangdong Province Engineering Laboratory for Marine Biological Products, Guangdong Ocean University, Zhanjiang 524088, China
Huina Zheng
College of Food Science and Technology, National Research and Development Branch Center for Shellfish Processing (Zhanjiang), Guangdong Provincial Key Laboratory of Aquatic Products Processing and Safety, Guangdong Provincial Engineering Technology Research Center of Seafood, Guangdong Province Engineering Laboratory for Marine Biological Products, Guangdong Ocean University, Zhanjiang 524088, China
Shaohe Xie
Guangdong Shaohe Pearl Co., Ltd., Shantou 515041, China
Pearl and nacre powders have been valuable traditional Chinese medicines with whitening properties for thousands of years. We utilized a high-temperature and high-pressure method along with compound enzyme digestion to prepare the enzymatic hydrolysates of nacre powder of Pinctada martensii (NP-PMH). The peptides were identified using LC–MS/MS and screened through molecular docking and molecular dynamics simulations. The interactions between peptides and tyrosinase were elucidated through enzyme kinetics, circular dichroism spectropolarimetry, and isothermal titration calorimetry. Additionally, their inhibitory effects on B16F10 cells were explored. The results showed that a tyrosinase-inhibitory peptide (Ala-His-Tyr-Tyr-Asp, AHYYD) was identified, which inhibited tyrosinase with an IC50 value of 2.012 ± 0.088 mM. The results of the in vitro interactions showed that AHYYD exhibited a mixed-type inhibition of tyrosinase and also led to a more compact enzyme structure. The binding reactions of AHYYD with tyrosinase were spontaneous, leading to the formation of a new set of binding sites on the tyrosinase. The B16F10 cell-whitening assay revealed that AHYYD could reduce the melanin content of the cells by directly inhibiting the activity of intracellular tyrosinase. Additionally, it indirectly affects melanin production by acting as an antioxidant. These results suggest that AHYYD could be widely used as a tyrosinase inhibitor in whitening foods and pharmaceuticals.
