Vallabhaneni S. Murthy
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Vallabhaneni S. Murthy has a total of 11 co-authors. Here are the top co-authors by number of shared publications:
- Alessandro Mugelli
Department of Neurosciences, Psychology, Drug Research and Child Health (NEUROFARBA), University of Florence, Florence, Italy
1 shared publication - Claudiu Trandafir Supuran
Department of NEUROFARBA, Section of Pharmaceutical and Nutraceutical Sciences, University of Florence, Polo Scientifico, Via U. Schiff 6, Sesto Fiorentino, Firenze, 50019, Italy
1 shared publication - Elisabetta Cerbai
Department of Neurosciences, Psychology, Drug Research and Child Health University of Florence Florence Italy
1 shared publication - Emanuela Berrino
Department of Drug Chemistry and Technologies, Sapienza University of Rome, P.le A. Moro 5, 00185 Rome, Italy
1 shared publication - Fabrizio Carta
Neurofarba Department, University of Florence
1 shared publication - Gianluca Bartolucci
Department of Neuroscience, Psychology, Drug Research and Child Health NEUROFARBA, University of Florence, 50139 Florence, Italy
1 shared publication
Latest Publications
- Open Access
Novel Sulfamide-Containing Compounds as Selective Carbonic Anhydrase I Inhibitors
The development of isoform selective inhibitors of the carbonic anhydrase (CA; EC 4.2.1.1) enzymes represents the key approach for the successful development of druggable small molecules. Herein we report a series of new benzenesulfamide derivatives (-NH-SO2NH2) bearing the 1-benzhydrylpiperazine tail and connected by means of a β-alanyl or nipecotyl spacer. All compounds 6a–l were investigated in vitro for their ability to inhibit the physiological relevant human (h) CA isoforms such as I, II, IV and IX. Molecular modeling provided further structural support to enzyme inhibition data and structure-activity relationship. In conclusion the hCA I resulted the most inhibited isoform, whereas all the remaining ones showed different inhibition profiles.
Open AccessNovel Sulfamide-Containing Compounds as Selective Carbonic Anhydrase I Inhibitors
The development of isoform selective inhibitors of the carbonic anhydrase (CA; EC 4.2.1.1) enzymes represents the key approach for the successful development of druggable small molecules. Herein we report a series of new benzenesulfamide derivatives (-NH-SO2NH2) bearing the 1-benzhydrylpiperazine tail and connected by means of a β-alanyl or nipecotyl spacer. All compounds 6a–l were investigated in vitro for their ability to inhibit the physiological relevant human (h) CA isoforms such as I, II, IV and IX. Molecular modeling provided further structural support to enzyme inhibition data and structure-activity relationship. In conclusion the hCA I resulted the most inhibited isoform, whereas all the remaining ones showed different inhibition profiles.