-Helical Peptide Containing N,N-Dimethyl Lysine Residues Displays Low-Nanomolar and Highly Specific Binding to RRE RNA
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- 作者：Soonsil Hyun ; Hyun Jin Kim ; Nam Ju Lee ; Kyung Hyun Lee ; Yeongran Lee ; Dae Ro Ahn ; Keysun Kim ; Sunjoo Jeong ; Jaehoon Yu
- 刊名：Journal of the American Chemical Society
- 出版年：2007
- 出版时间：April 18, 2007
- 年：2007
- 卷：129
- 期：15
- 页码：4514 - 4515
- 全文大小：28K
- 年卷期：v.129,no.15(April 18, 2007)
- ISSN：1520-5126
文摘
The combinatorial introduction of N,N-dimethyl-Lys groups into Lys-rich 
-helical peptides and measuring affinities against RRE RNA were carried out. Peptide-g, in which two Lys were replaced by N,N-dimethyl-Lys at 3 and 9 positions, showed low-nanomolar affinity, which is almost the same value as Rev peptide, the natural RRE ligand. Moreover, peptide-g displays a compatible binding specificity as Rev peptide. The effects of the positions of Lys N,N-dimethylation on the specificity of RNA binding could serve as the basis of a new strategy for the design of novel agents against RNAs. The results support that nature may use N-methylation as a post-translational modification to enhance specific peptide-RNA interactions.
-helical peptides and measuring affinities against RRE RNA were carried out. Peptide-g, in which two Lys were replaced by N,N-dimethyl-Lys at 3 and 9 positions, showed low-nanomolar affinity, which is almost the same value as Rev peptide, the natural RRE ligand. Moreover, peptide-g displays a compatible binding specificity as Rev peptide. The effects of the positions of Lys N,N-dimethylation on the specificity of RNA binding could serve as the basis of a new strategy for the design of novel agents against RNAs. The results support that nature may use N-methylation as a post-translational modification to enhance specific peptide-RNA interactions.© 2004-2018 中国地质图书馆版权所有 京ICP备05064691号 京公网安备11010802017129号 地址：北京市海淀区学院路29号 邮编：100083 电话：办公室：(+86 10)66554848；文献借阅、咨询服务、科技查新：66554700 |