Abstract
Correlation Between Physico-Chemical Properties And Protein Binding Of Phenothiazine Derivatives
The binding of a series of phenothiazine derivatives to bovine serum albumin was Investigated using fluorescene spectroscopic technique. In an attempt to elucidate the binding mechanism and to predict binding affinity, association constants for drug-protein binding have been correlated to physico-chemical parameters by fitting linear, multiple linear and quardratic equations to the data. The rationale of including molecular weight and molecular volume terms in the quantitative structure-activity correlations has been emphasized. It has been concluded that binding primarily involves hydrophobicity and molecular size of drug cations. However, the role of electrostatic forces as measured by ionization constant, pKa and molar conductance cannot be ignored. The association constants could be predicted with a fair degree of accuracy from physico-chemical properties of the drug molecules.
