Open AccessPeptides Mimicking the β7/β8 Loop of HIV-1 Reverse Transcriptase p51 as “Hotspot-Targeted” Dimerization Inhibitors
Author(s) -
Pedro A. SánchezMurcia,
Sonia de Castro,
Carlos Garcı́a-Aparicio,
María Ángeles Sánchez Jiménez,
Angela Corona,
Enzo Tramontano,
Nicolas SluisCremer,
Luis MenéndezArias,
Sonsoles Velázquez,
Federico Gago,
MaríaJosé Camarasa
Publication year - 2020
Publication title -
acs medicinal chemistry letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.065
H-Index - 66
ISSN - 1948-5875
DOI - 10.1021/acsmedchemlett.9b00623
Subject(s) - reverse transcriptase , human immunodeficiency virus (hiv) , peptide , chemistry , computational biology , hotspot (geology) , bioinformatics , combinatorial chemistry , virology , biology , biochemistry , rna , physics , gene , geophysics
A conformationally constrained short peptide designed to target a protein-protein interaction hotspot in HIV-1 reverse transcriptase (RT) disrupts p66-p51 interactions and paves the way to the development of novel RT dimerization inhibitors.