Titolo:  Exploring new scaffolds for the dual inhibition of HIV-1 RT polymerase and ribonuclease associated functions
Data di pubblicazione:  2021
Data di prima pubblicazione on-line:  2021
Autori:  Meleddu, Rita; Corona, Angela; Distinto, Simona; Cottiglia, Filippo; Deplano, Serenella; Sequeira, Lisa; Secci, Daniela; Onali, Alessia; Sanna, Erica; Esposito, Francesca; Cirone, Italo; Ortuso, Francesco; Alcaro, Stefano; Tramontano, Enzo; Mátyus, Péter; Maccioni, Elias
Numero degli autori:  16
Lingua:  Inglese
Presenza coautori internazionali: 
Volume:  26
Fascicolo:  13
Numero dell’articolo:  3821
Pagina iniziale:  1
Pagina finale:  16
Numero di pagine:  16
Digital Object Identifier (DOI):  http://dx.doi.org/10.3390/molecules26133821
Codice identificativo Pubmed:  34201561
Codice identificativo Scopus:  2-s2.0-85109180628
Codice identificativo ISI:  WOS:000671213800001
Abstract:  Current therapeutic protocols for the treatment of HIV infection consist of the combination of diverse anti-retroviral drugs in order to reduce the selection of resistant mutants and to allow for the use of lower doses of each single agent to reduce toxicity. However, avoiding drugs interactions and patient compliance are issues not fully accomplished so far. Pursuing on our investigation on potential anti HIV multi-target agents we have designed and synthesized a small library of biphenylhydrazo 4-arylthiazoles derivatives and evaluated to investigate the ability of the new derivatives to simultaneously inhibit both associated functions of HIV reverse transcriptase. All compounds were active towards the two functions, although at different concentrations. The substitution pattern on the biphenyl moiety appears relevant to determine the activity. In particular, compound 2-{3- [(2-{4-[4-(hydroxynitroso)phenyl]-1,3-thiazol-2-yl} hydrazin-1-ylidene) methyl]-4-methoxyphenyl} benzamide bromide (EMAC2063) was the most potent towards RNaseH (IC50 = 4.5 mM)- and RDDP (IC50 = 8.0 mM) HIV RT-associated functions
Parole chiave:  HIV-RT; ribonuclease H; dual inhibitors; docking; putative binding
Tipologia: 1.1 Articolo in rivista

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