Abstract
Among all the malaria parasites, P. falciparum is the most predominant species which has developed drug resistance against most of the commercial anti-malarial drugs. Thus, finding a new molecule for the inhibition of enzymes of P. falciparum is the pharmacological challenge in present era. Herein, ten novel molecules have been designed with an amalgamation of cinchonidine, carbohydrate moiety and triazole ring by utilizing copper-catalyzed click reaction of cinchonidine-derived azide and clickable glycosyl alkynes. The molecular docking of developed molecules showed promising results for plasmepsin inhibition in the form of effective binding with target proteins.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Antimalarials / chemical synthesis*
-
Antimalarials / chemistry
-
Antimalarials / pharmacology
-
Aspartic Acid Endopeptidases / antagonists & inhibitors*
-
Aspartic Acid Endopeptidases / chemistry
-
Catalysis
-
Cinchona Alkaloids / chemical synthesis
-
Cinchona Alkaloids / chemistry*
-
Cinchona Alkaloids / pharmacology
-
Click Chemistry
-
Copper / chemistry
-
Drug Design
-
Humans
-
Malaria, Falciparum / parasitology
-
Molecular Docking Simulation
-
Molecular Structure
-
Plasmodium falciparum / drug effects*
-
Plasmodium falciparum / enzymology
-
Protease Inhibitors / chemical synthesis*
-
Protease Inhibitors / chemistry
-
Protease Inhibitors / pharmacology
-
Protozoan Proteins / antagonists & inhibitors*
-
Protozoan Proteins / chemistry
-
Triazoles / chemistry
Substances
-
Antimalarials
-
Cinchona Alkaloids
-
Protease Inhibitors
-
Protozoan Proteins
-
Triazoles
-
cinchonidine
-
Copper
-
Aspartic Acid Endopeptidases
-
plasmepsin