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Constrained peptidomimetics as antiplasmodial falcipain-2 inhibitors.
- Source :
-
Bioorganic & medicinal chemistry [Bioorg Med Chem] 2010 Jul 15; Vol. 18 (14), pp. 4928-38. Date of Electronic Publication: 2010 Jun 10. - Publication Year :
- 2010
-
Abstract
- Herein we report the synthesis of a series of novel constrained peptidomimetics 2-10 endowed with a dipeptide backbone (D-Ser-Gly) and a vinyl ester warhead, structurally related to a previously identified lead compound 1, an irreversible inhibitor of falcipain-2, the main haemoglobinase of lethal malaria parasite Plasmodium falciparum. The new compounds were evaluated for their inhibition against falcipain-2, as well as against cultured P. falciparum. The inhibitory activity of the synthesized compounds was also evaluated against another protozoal cysteine protease, namely rhodesain of Trypanosoma brucei rhodesiense.<br /> (Copyright (c) 2010 Elsevier Ltd. All rights reserved.)
- Subjects :
- Humans
Trypanosoma brucei rhodesiense drug effects
Trypanosoma brucei rhodesiense enzymology
Trypanosomiasis, African drug therapy
Antiprotozoal Agents chemistry
Antiprotozoal Agents pharmacology
Cysteine Endopeptidases metabolism
Malaria, Falciparum drug therapy
Peptides chemistry
Peptides pharmacology
Plasmodium falciparum drug effects
Plasmodium falciparum enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1464-3391
- Volume :
- 18
- Issue :
- 14
- Database :
- MEDLINE
- Journal :
- Bioorganic & medicinal chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 20598553
- Full Text :
- https://doi.org/10.1016/j.bmc.2010.06.010