ArticleMolecular diversity2019
Structural characterization of plasmodial aminopeptidase: a combined molecular docking and QSAR-based in silico approaches.
Article in Molecular diversity, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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3 authors at 2 institutions in 1 country.
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Abstract
Aminopeptidase M1 (PfAM1) is one of the key enzymes involved in the development of new antimalarials. To accelerate the discovery of inhibitors with selective activity against PfAM1 and microsomal neutral aminopeptidase (pAPN), in the present work, the optimum comparative molecular field analysis (CoMFA) and comparative molecular similarity indices analysis (CoMSIA) models were built based on PfAM1 and pAPN inhibitors. The results of the developed 3D-QSAR models were as follows: PfAM1/CoMFA: [Formula: see text] = 0.740, [Formula: see text] = 0.7781; PfAM1/CoMSIA: [Formula: see text] = 0.740, [Formula: see text] = 0.7354; pAPN/CoMFA: [Formula: see text] = 0.612, [Formula: see text] = 0.7318; pAPN/CoMSIA: [Formula: see text] = 0.609, [Formula: see text] = 0.7480, and the models derived from MLR, PLSR and SVR methods provided high R
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