1350906-14-7Relevant articles and documents
Development of a Raltegravir-based Photoaffinity-Labeled Probe for Human Immunodeficiency Virus-1 Integrase Capture
Pala, Nicolino,Esposito, Francesca,Tramontano, Enzo,Singh, Pankaj Kumar,Sanna, Vanna,Carcelli, Mauro,Haigh, Lisa D.,Satta, Sandro,Sechi, Mario
, p. 1986 - 1992 (2020)
Photoaffinity labeling (PAL) is one of the upcoming and powerful tools in the field of molecular recognition. It includes the determination of dynamic parameters, such as the identification and localization of the target protein and the site of drug binding. In this study, a photoaffinity-labeled probe for full-length human immunodeficiency virus-1 integrase (HIV-1 IN) capture was designed and synthesized, following the structure of the FDA-approved drug Raltegravir. This photoprobe was found to retain the HIV IN inhibitory potential in comparison with its parent molecule and demonstrates the ability to label the HIV-1 IN protein. Putative photoprobe/inhibitor binding sites near the catalytic site were then identified after protein digestion coupled to mass and molecular modeling analyses.
Investigating the role of metal chelation in HIV-1 integrase strand transfer inhibitors
Bacchi, Alessia,Carcelli, Mauro,Compari, Carlotta,Fisicaro, Emilia,Pala, Nicolino,Rispoli, Gabriele,Rogolino, Dominga,Sanchez, Tino W.,Sechi, Mario,Sinisi, Valentina,Neamati, Nouri
experimental part, p. 8407 - 8420 (2012/02/14)
HIV-1 integrase (IN) has been validated as an attractive target for the treatment of HIV/AIDS. Several studies have confirmed that the metal binding function is a crucial feature in many of the reported IN inhibitors. To provide new insights on the metal
