Related Experiment Video
Updated: Jul 6, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates
Published on: February 27, 2016
Structure function analysis of Leishmania sirtuin: an ensemble of in silico and biochemical studies
Rameshwar U Kadam1, Joana Tavares1, Kiran V M1
1Centre of Pharmacoinformatics, National Institute of Pharmaceutical Education and Research, Sector 67, S.A.S Nagar-160062, Punjab, IndiaIBMC, Instituto de Biologia Molecular e Celular da Universidade do Porto, PortugalFaculdade de Farmacia da Universidade do Porto, PortugalINSERM, Institut National de la Santé et de la Recherche Médicale, FranceIRD, UR008 'Pathogenie des Trypanosomatides', 911 Avenue Agropolis, BP 64501, 34394 Montpellier Cedex 5, France.
Abstract:
Novel anti-leishmanial target LmSir2 has few subtle but prudent structural differences in ligand binding and catalytic domain as compared to its human counterpart. In silico screening and validation followed by in vitro deacetylation and cell killing assays described herein give a proof of concept for development of strategies exploiting such minor differences for screening libraries of small molecules to identify selective inhibitors.
Related Concept Videos
Antiprotozoal Agents
Ligand Binding Sites
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

