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QSAR of Aromatic Substances: Protein Tyrosine Kinase Inhibitory Activity of Flavonoid Analogues
Author(s) -
Deeb Omar,
Clare Brian W.
Publication year - 2007
Publication title -
chemical biology and drug design
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.59
H-Index - 77
eISSN - 1747-0285
pISSN - 1747-0277
DOI - 10.1111/j.1747-0285.2007.00578.x
Subject(s) - chemistry , flavonoid , stereochemistry , quantitative structure–activity relationship , inhibitory postsynaptic potential , atomic orbital , computational chemistry , active site , enzyme , biochemistry , biology , antioxidant , physics , quantum mechanics , neuroscience , electron
The flip regression procedure that we used earlier for handling xanthones (J Enzyme Inhib Med Chem;22:277, 2006) has been applied to flavonoid analogues. It is demonstrated that the electrostatic and quantum chemical descriptors for the interaction of flavonoids with the specific enzymatic active site plays an important role. In particular, the maximal total interaction for a C–O bond is the most important factor in the regression. In this contribution it is shown that the orientation of nodes in their occupied π orbitals, and also the energies of these orbitals explain a further large portion of the variance in their inhibitory activity.