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Amphiphilic Helical Peptides Containing Two Acridine Moieties Display Picomolar Affinity toward HIV‐1 RRE and TAR
Author(s) -
Lee Yeongran,
Hyun Soonsil,
Kim Hyun Jin,
Yu Jaehoon
Publication year - 2007
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200703090
Subject(s) - acridine , affinities , binding affinities , pharmacophore , chemistry , amphiphile , rna , hydrogen bond , combinatorial chemistry , tar (computing) , human immunodeficiency virus (hiv) , intercalation (chemistry) , stereochemistry , biophysics , biochemistry , molecule , organic chemistry , biology , computer science , copolymer , receptor , immunology , gene , programming language , polymer
Hold on tight : Amphiphilic α‐helical peptides that contain acridine moieties were synthesized, and their binding affinities toward hairpin RNA targets were evaluated. The dramatic increase in binding affinities (40‐fold for RRE, 170‐fold for TAR) demonstrates that conjugation of intercalators that operate by different binding modes (ionic or hydrogen bonding) leads to one of the most tightly binding pharmacophores against RNA targets.