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Exploration of Sitagliptin as a Potential Inhibitor for the M1 Alanine Aminopeptidase Enzyme in Plasmodium Falciparum Using Computational Docking

Exploration of Sitagliptin as a Potential Inhibitor for the M1 Alanine Aminopeptidase Enzyme in Plasmodium Falciparum Using Computational Docking

Mohana Krishnamoorthy, Anant Achary

Bioinformation. 2013;9(6):293-8.

PMID: 23559748

Abstract:

Plasmodium falciparum has limited capacity for de novo amino acid synthesis and rely on degradation of host hemoglobin to maintain protein metabolism and synthesis of proteins. M1 alanine aminopeptidase enzyme of the parasite involved in the terminal degradation of host hemoglobin was subjected to in silico screening with low molecular weight protease inhibitors. The km (avg) of the enzyme M1 alanine aminopeptidase for the substrate DL - Alanine β Napthylamide Hydrochloride was estimated as 322.05µM. The molecular interactions between the enzyme and the substrate and the mechanism of enzyme action were analyzed which paved way for inhibition strategies. Among all the inhibitors screened, Sitagliptin was found to be most potent inhibitor with ki of 0.152 µM in its best orientation whereas the ki(avg) was 2.0055 µM. The ki of Sitagliptin is lower than the km of M1 alanine aminopeptidase for the substrate DL - Alanine β Napthylamide Hydrochloride (322.05 µM) and Ki of the known inhibitor Bestatin. Therefore Sitagliptin may serve as a potent competitive inhibitor of the enzyme M1 alanine aminopeptidase of Plasmodium falciparum.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP65391426	Bestatin hydrochloride		65391-42-6	Price

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