Bhaskar R. Shenai
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Bhaskar R. Shenai has a total of 7 co-authors. Here are the top co-authors by number of shared publications:
Alejandro Alvarez-Hernandez
Department of Medicine, San Francisco General Hospital, University of California, San Francisco, California,1 Department of Chemistry, University of Michigan, Ann Arbor, Michigan2
1 shared publicationBelinda J. Lee
Department of Medicine, San Francisco General Hospital, University of California, San Francisco, California,1 Department of Chemistry, University of Michigan, Ann Arbor, Michigan2
1 shared publicationCory D. Emal
Department of Medicine, San Francisco General Hospital, University of California, San Francisco, California,1 Department of Chemistry, University of Michigan, Ann Arbor, Michigan2
1 shared publicationPek Y. Chong
Department of Medicine, San Francisco General Hospital, University of California, San Francisco, California,1 Department of Chemistry, University of Michigan, Ann Arbor, Michigan2
1 shared publicationPhilip J. Rosenthal
Department of Medicine, San Francisco General Hospital, University of California, San Francisco, California,1 Department of Chemistry, University of Michigan, Ann Arbor, Michigan2
1 shared publicationR. Jeffrey Neitz
Department of Medicine, San Francisco General Hospital, University of California, San Francisco, California,1 Department of Chemistry, University of Michigan, Ann Arbor, Michigan2
1 shared publication
Latest Publications
- Open Access
- 1 January 2003
- Published by American Society for Microbiology in Antimicrobial Agents and Chemotherapy
- Vol. 47 (1) , 154-160
Structure-Activity Relationships for Inhibition of Cysteine Protease Activity and Development of Plasmodium falciparum by Peptidyl Vinyl Sulfones
The Plasmodium falciparum cysteine proteases falcipain-2 and falcipain-3 appear to be required for hemoglobin hydrolysis by intraerythrocytic malaria parasites. Previous studies showed that peptidyl vinyl sulfone inhibitors of falcipain-2 blocked the development of P. falciparum in culture and exerted antimalarial effects in vivo. We now report the structure-activity relationships for inhibition of falcipain-2, falcipain-3, and parasite development by 39 new vinyl sulfone, vinyl sulfonate ester, and vinyl sulfonamide cysteine protease inhibitors. Levels of inhibition of falcipain-2 and falcipain-3 were generally similar, and many potent compounds were identified. Optimal antimalarial compounds, which inhibited P. falciparum development at low nanomolar concentrations, were phenyl vinyl sulfones, vinyl sulfonate esters, and vinyl sulfonamides with P 2 leucine moieties. Our results identify independent structural correlates of falcipain inhibition and antiparasitic activity and suggest that peptidyl vinyl sulfones have promise as antimalarial agents.
- 1 January 2003
- Published by American Society for Microbiology in Antimicrobial Agents and Chemotherapy
- Vol. 47 (1) , 154-160
Open AccessStructure-Activity Relationships for Inhibition of Cysteine Protease Activity and Development of Plasmodium falciparum by Peptidyl Vinyl Sulfones
The Plasmodium falciparum cysteine proteases falcipain-2 and falcipain-3 appear to be required for hemoglobin hydrolysis by intraerythrocytic malaria parasites. Previous studies showed that peptidyl vinyl sulfone inhibitors of falcipain-2 blocked the development of P. falciparum in culture and exerted antimalarial effects in vivo. We now report the structure-activity relationships for inhibition of falcipain-2, falcipain-3, and parasite development by 39 new vinyl sulfone, vinyl sulfonate ester, and vinyl sulfonamide cysteine protease inhibitors. Levels of inhibition of falcipain-2 and falcipain-3 were generally similar, and many potent compounds were identified. Optimal antimalarial compounds, which inhibited P. falciparum development at low nanomolar concentrations, were phenyl vinyl sulfones, vinyl sulfonate esters, and vinyl sulfonamides with P 2 leucine moieties. Our results identify independent structural correlates of falcipain inhibition and antiparasitic activity and suggest that peptidyl vinyl sulfones have promise as antimalarial agents.