A Novel Heptapeptide with Tyrosinase Inhibitory Activity Identified from a Phage Display Library

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• 作者：Huali Nie ; Lin Liu ; Huiqin Yang ; Hongzhen Guo…
• 关键词：Mushroom tyrosinase ; Inhibition ; Heptapeptide ; Phage display ; Molecular docking
• 刊名：Applied Biochemistry and Biotechnology
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：181
• 期：1
• 页码：219-232
• 全文大小：
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Biotechnology; Biochemistry, general;
• 出版者：Springer US
• ISSN：1559-0291
• 卷排序：181

文摘

Peptidic inhibition of the enzyme tyrosinase, responsible for skin pigmentation and food browning, would be extremely useful for the food, cosmetics, and pharmaceutical industries. In order to identify novel inhibitory peptides, a library of short sequence oligopeptides was screened to reveal direct interaction with the tyrosinase. A phage displaying heptapeptide (IQSPHFF) was found to bind most strongly to tyrosinase. The inhibitory activity of the heptapeptide was evaluated using mushroom tyrosinase. The results showed that the peptide inhibited both the monophenolase and diphenolase activities of mushroom tyrosinase with IC₅₀ values of 1.7 and 4.0 mM, respectively. The heptapeptide is thought to be a reversible competitive inhibitor of diphenolase with the inhibition constants (Ki) of 0.765 mM. To further investigate how the heptapeptide exerts its inhibitory effect, a docking study between tyrosinase and heptapeptide was performed. The simulation showed that the heptapeptide binds in the active site of the enzyme near the catalytically active Cu ions and forms hydrogen bonds with five histidine residues on the active site. Phage display technology is thus a useful approach for the screening of potential tyrosinase inhibitors and could be widely applicable to a much wider range of enzymes.