In Vitro In Silico Screening Strategy and Mechanism of Novel Tyrosinase Inhibitory Peptides from Nacre of Hyriopsis cumingii

IF 4.9 2区医学 Q1 CHEMISTRY, MEDICINAL

Marine Drugs Pub Date : 2024-09-15 DOI:10.3390/md22090420

Haisheng Lin, Fei Li, Jiaao Kang, Shaohe Xie, Xiaoming Qin, Jialong Gao, Zhongqin Chen, Wenhong Cao, Huina Zheng, Wenkui Song

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Abstract

For thousands of years, pearl and nacre powders have been important traditional Chinese medicines known for their skin whitening effects. To prepare the enzymatic hydrolysates of Hyriopsis cumingii nacre powder (NP-HCH), complex enzymatic hydrolysis by pineapple protease and of neutral protease was carried out after the powder was pre-treated with a high-temperature and high-pressure method. The peptides were identified using LC-MS/MS and picked out through molecular docking and molecular dynamics simulations. Subsequently, the tyrosinase inhibitory and antioxidant properties of novel tyrosinase inhibitory peptides were investigated in vitro. In addition, the enzymatic activity of tyrosinase in B16F10 cells as well as melanin content and antioxidant enzyme levels were also examined. The results showed that a tyosinase inhibitory peptide (Tyr-Pro-Asn-Pro-Tyr, YPNPY) with an efficient IC50 value of 0.545 ± 0.028 mM was identified. The in vitro interaction results showed that YPNPY is a reversible competitive inhibitor of tyrosinase, suggesting that it binds to the free enzyme. The B16F10 cell whitening test revealed that YPNPY can reduce the melanin content of B16F10 cells by directly inhibiting the activity of intracellular tyrosinase. Additionally, it indirectly affects melanin production by acting as an antioxidant. These results suggest that YPNPY could be widely used as a tyrosinase inhibitor in whitening foods and drugs.

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新型酪氨酸酶抑制肽的体外硅学筛选策略与机制

数千年来，珍珠和珍珠粉一直是重要的传统中药，以其美白功效而闻名。为了制备拟南芥珍珠粉（NP-HCH）的酶水解物，在对珍珠粉进行高温高压预处理后，采用菠萝蛋白酶和中性蛋白酶进行复合酶水解。利用 LC-MS/MS 对肽段进行了鉴定，并通过分子对接和分子动力学模拟对肽段进行了筛选。随后，在体外研究了新型酪氨酸酶抑制肽的酪氨酸酶抑制和抗氧化特性。此外，还检测了 B16F10 细胞中酪氨酸酶的酶活性以及黑色素含量和抗氧化酶水平。结果表明，找到了一种抑制酪氨酸酶的多肽（Tyr-Pro-Asn-Pro-Tyr，YPNPY），其有效 IC50 值为 0.545 ± 0.028 mM。体外相互作用结果表明，YPNPY 是一种可逆的酪氨酸酶竞争性抑制剂，表明它能与游离酶结合。B16F10 细胞增白试验表明，YPNPY 可直接抑制细胞内酪氨酸酶的活性，从而降低 B16F10 细胞的黑色素含量。此外，它还能作为一种抗氧化剂间接影响黑色素的生成。这些结果表明，YPNPY 可作为一种酪氨酸酶抑制剂广泛应用于美白食品和药物中。

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来源期刊

Marine Drugs 医学-医药化学

CiteScore

9.60

自引率

14.80%

发文量

671

审稿时长

1 months

期刊介绍： Marine Drugs (ISSN 1660-3397) publishes reviews, regular research papers and short notes on the research, development and production of drugs from the sea. Our aim is to encourage scientists to publish their experimental and theoretical research in as much detail as possible, particularly synthetic procedures and characterization information for bioactive compounds. There is no restriction on the length of the experimental section.