α-helical peptide containing N,N-dimethyl lysine residues displays low-nanomolar and highly specific binding to RRE RNA
α-helical peptide containing N,N-dimethyl lysine residues displays low-nanomolar and highly specific binding to RRE RNA
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DOI：
10.1021/ja068265m
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发表时间：
2007-04-18
影响因子：
15
通讯作者：
Yu, Jaehoon
中科院分区：
文献类型：
--
作者：
Hyun, Soonsil;Kim, Hyun Jin;Yu, Jaehoon
进行了将N，N-二甲基-赖氨酸基团组合引入富含赖氨酸的α-螺旋肽并测量对RRE RNA的亲和力。肽-g，其中两个赖氨酸被取代的N，N-二甲基-赖氨酸在3和9位，显示出低纳摩尔的亲和力，这是几乎相同的值作为Rev肽，天然RRE配体。此外，肽-g显示出与Rev肽相容的结合特异性。赖氨酸N，N-二甲基化位置对RNA结合特异性的影响可以作为设计针对RNA的新型药物的新策略的基础。结果支持自然界可能使用N-甲基化作为翻译后修饰来增强特定肽-RNA相互作用。
The combinatorial introduction of N,N-dimethyl-Lys groups into Lys-rich alpha-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.