Keywords

Synthase, Ts), Mrna In Vitro Display, Screening, Affinity Peptide, Thymidylate Synthase (Thymidylate

Abstract

Thymidylatesynthase (TS) is an enzyme necessary for catalyzing the synthesis of thymidylate in organisms. It has been used as a target for tumor chemotherapy for many years. Studies have shown that TS is an RNA-binding protein that can interact with its own mRNA. Binding to a site blocks the translation of mRNA. This article used in vitro mRNA display technology to screen thymidylate synthase mRNA affinity peptides from a large-capacity peptide library (>1013), and conducted 12 rounds of random library testing. Selection and amplification. The results show that compared with the initial library, after selection cycles, the content of basic amino acids and aromatic phenylalanine increased significantly, and they play an important role in the interaction between TSRNA and proteins. According to its Physicochemical properties were used to classify the amino acids at each random position and compared with the initial library. It was found that positions 1, 12, 17 and 18 have obvious positively charged characteristics, indicating that the basic side chain is involved in binding to RNA. Secondary structure prediction showed that as the screening progressed, the polypeptides with affinity to TSmRNA showed obvious helical tendencies, and the regions forming helices were rich in basic amino acids. Gel migration and in vitro translation experiments confirmed that the polypeptides after selection cycle It has high affinity to TSmRNA and can inhibit the translation of TSmRNA. This study shows that the affinity peptide obtained by the in vitro mRNA display method can be used as a new TSRNA translation inhibitor and may become a new type of anti-tumor drug.

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Original research done by Yan Song, Niu Rongli, Wang Zheng, Lin Xiukun

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