Reviewing ligand-based rational drug design: the search for an ATP synthase inhibitor.
Journal
International Journal of Molecular Sciences
Journal Volume
12
Journal Issue
8
Pages
5304-5318
Date Issued
2011
Author(s)
Abstract
Following major advances in the field of medicinal chemistry, novel drugs can now be designed systematically, instead of relying on old trial and error approaches. Current drug design strategies can be classified as being either ligand- or structure-based depending on the design process. In this paper, by describing the search for an ATP synthase inhibitor, we review two frequently used approaches in ligand-based drug design: The pharmacophore model and the quantitative structure-activity relationship (QSAR) method. Moreover, since ATP synthase ligands are potentially useful drugs in cancer therapy, pharmacophore models were constructed to pave the way for novel inhibitor designs. ? 2011 by the authors; licensee MDPI, Basel, Switzerland.
Subjects
ATP synthase ligands; Pharmacophore; Quantitative structure-activity relationships
SDGs
Other Subjects
adenosine triphosphatase inhibitor; asteltoxin; aurovertin b; bathophenanthroline; citreoviridin; enterostatin; ligand; mepacrine mustard; piceatannol; proton transporting adenosine triphosphate synthase inhibitor; resveratrol; unclassified drug; enzyme inhibitor; protein binding; protein subunit; proton transporting adenosine triphosphate synthase; binding site; cancer therapy; computer aided design; drug design; drug protein binding; drug structure; hydrogen bond; intermethod comparison; ligand binding; molecular docking; pharmacophore; prediction; process optimization; quantitative structure activity relation; review; scoring system; surface property; three dimensional imaging; validation process; antagonists and inhibitors; chemical phenomena; chemical structure; chemistry; human; metabolism; protein subunit; Binding Sites; Drug Design; Enzyme Inhibitors; Humans; Hydrophobic and Hydrophilic Interactions; Ligands; Mitochondrial Proton-Translocating ATPases; Models, Molecular; Protein Binding; Protein Subunits; Quantitative Structure-Activity Relationship
Publisher
MDPI
Type
journal article