Identification of peptides that bind with thymidylate synthase RNA using mRNA display technique
Yan, S; Niu, RL; Zhang, PJ; Lin, XK
刊名PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS
2005-11-01
卷号32期号:11页码:1081-1087
关键词In Vitro Mrna Display Selection Thymidylate Synthase Affinity Peptides
ISSN号1000-3282
文献子类Article
英文摘要Using in vitro selection method to isolate nucleic acids, peptides and proteins has been studied intensively in recent years. In vitro mRNA display is a new and effective technique for peptides selection, and the rationale of this technique is that a synthetic mRNA with puromycin could covalently link with the protein that it encodes, thus an mRNA-protein fusion is formed. This approach has been used in identification of many functional peptides. The peptides binding with thymidylate synthase RNA were isolated using mRNA display technique from a large peptide library (>10(13) different sequences). The selection scheme was constructed, and the experimental conditions, including library synthesis, formation of RNA-peptide fusion and RNA immobilization were optimized. Eight cycles have been processed and the results confirmed that the selected peptides could bind with thymidylate synthase mRNA specifically. Compared the amino acid sequences of the selected peptides with those from the initial random library, the basic and aromatic residues in selected peptides were enriched significantly, suggesting these peptide regions may be important in the peptide-TS mRNA interaction. As a novel in vitro selection approach, mRNA display technique would be developed as a powerful tool for isolation of functional peptides and proteins that could interact with immobilized targets with high affinity and specificity.; Using in vitro selection method to isolate nucleic acids, peptides and proteins has been studied intensively in recent years. In vitro mRNA display is a new and effective technique for peptides selection, and the rationale of this technique is that a synthetic mRNA with puromycin could covalently link with the protein that it encodes, thus an mRNA-protein fusion is formed. This approach has been used in identification of many functional peptides. The peptides binding with thymidylate synthase RNA were isolated using mRNA display technique from a large peptide library (>10(13) different sequences). The selection scheme was constructed, and the experimental conditions, including library synthesis, formation of RNA-peptide fusion and RNA immobilization were optimized. Eight cycles have been processed and the results confirmed that the selected peptides could bind with thymidylate synthase mRNA specifically. Compared the amino acid sequences of the selected peptides with those from the initial random library, the basic and aromatic residues in selected peptides were enriched significantly, suggesting these peptide regions may be important in the peptide-TS mRNA interaction. As a novel in vitro selection approach, mRNA display technique would be developed as a powerful tool for isolation of functional peptides and proteins that could interact with immobilized targets with high affinity and specificity.
学科主题Biochemistry & Molecular Biology ; Biophysics
语种英语
WOS记录号WOS:000233534300013
公开日期2010-12-22
内容类型期刊论文
源URL[http://ir.qdio.ac.cn/handle/337002/3149]  
专题海洋研究所_实验海洋生物学重点实验室
作者单位1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
2.Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China
3.Yale Univ, Sch Med, Dept Med & Pharmacol, New Haven, CT 06520 USA
推荐引用方式
GB/T 7714
Yan, S,Niu, RL,Zhang, PJ,et al. Identification of peptides that bind with thymidylate synthase RNA using mRNA display technique[J]. PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS,2005,32(11):1081-1087.
APA Yan, S,Niu, RL,Zhang, PJ,&Lin, XK.(2005).Identification of peptides that bind with thymidylate synthase RNA using mRNA display technique.PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS,32(11),1081-1087.
MLA Yan, S,et al."Identification of peptides that bind with thymidylate synthase RNA using mRNA display technique".PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS 32.11(2005):1081-1087.
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