Hyun, Soonsil Kim, Hyun Jin Lee, Nam Ju Lee, Kyung Hyun Lee, Yeongran Ahn, Dae Ro Kim, Keysun Jeong, Sunjoo Yu, Jaehoon 2024-01-21T01:05:19Z 2024-01-21T01:05:19Z 2021-09-02 2007-04 0002-7863 https://pubs.kist.re.kr/handle/201004/134494 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. English AMER CHEMICAL SOC alpha-helical peptide containing N,N-dimethyl lysine residues displays low-nanomolar and highly specific binding to RRE RNA Article 10.1021/ja068265m 1 JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, v.129, no.15, pp.4514 - + JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 129 15 4514 + N scie scopus 000245739700005 2-s2.0-34247481379 Chemistry, Multidisciplinary Chemistry Article BETA-HAIRPIN PEPTIDE HIV-1 REV ARGININE METHYLATION PI INTERACTIONS AMINO-ACIDS CONSTRUCTION SEQUENCE AFFINITY GENOME ARG alpha-helical peptide RRE RNA dimethyl lysine