Cover Picture: Studies on Cycloheptathiophene‐3‐carboxamide Derivatives as Allosteric HIV‐1 Ribonuclease H Inhibitors (ChemMedChem 16/2016). (19th August 2016)

• Record Type: Journal Article
• Authors: Corona, Angela; Desantis, Jenny; Massari, Serena; Distinto, Simona; Masaoka, Takashi; Sabatini, Stefano; Esposito, Francesca; Manfroni, Giuseppe; Maccioni, Elias; Cecchetti, Violetta; Pannecouque, Christophe; Le Grice, Stuart F. J.; Tramontano, Enzo; Tabarrini, Oriana
• Is Part Of: ChemMedChem. Volume 11:Number 16(2016)
• Page Start: 1669
• Page End: 1669
• Publication Date: 2016-08-19
• Subjects: allosterism antiviral agents inhibitors medicinal chemistry ribonucleases; Pharmaceutical chemistry -- Periodicals; 615.19005
• DOI: 10.1002/cmdc.201600392
• Languages: English
• ISSNs: 1860-7179

Abstract

Abstract : The front cover picture shows the heterodimeric structure of the HIV‐1 reverse transcriptase (RT) complexed with the RNA:DNA duplex. RT is a multifunctional enzyme endowed with several different functions, including the ribonuclease H (RNase H) activity responsible for the RNA strand hydrolysis of the RNA:DNA replication intermediate. Compounds able to interfere with this pivotal RT‐associated function could represent an innovative anti‐HIV‐1 strategy. The cycloheptathiophene‐3‐carboxamide catechol derivative is a new RNase H nanomolar inhibitor, which is able to recognize an allosteric site (yellow) located below the catalytic site (light blue) as suggested by computational studies. More information can be found in the Full Paper by Oriana Tabarrini, et al. onpage 1709 in Issue 16, 2016 (DOI:10.1002/cmdc.201600015 ). Artwork by Serena Massari.