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2 Acta Biochimica Polonica

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An approach based on diffusion to study ligand-macromolecule interaction.

100%

Housaindokht M. R. , Bahrololoom M. , Tarighatpoor S. , Mossavi-Movahedi A. A.

Acta Biochimica Polonica

2002

tom 49

nr 3

703-707

A new approach has been developed to study binding of a ligand to a macromolecule based on the diffusion process. In terms of the Fick's first law, the concentration of free ligand in the presence of a protein can be determined by the measurement of those ligands which are diffused out. This method is applied to the study of binding of methyl-orange to lysozyme in phosphate buffer of pH 6.2, at 30°C. The binding isotherm was determined initially, followed by application of the Hill equation to the data obtained, then binding constant and binding capacity were estimated.

Targeting drug-efflux pumps - a pharmacoinformatic approach

75%

Pleban K. , Kaiser D. , Kopp S. , Peer M. , Chiba P. , Ecker G. F.

Acta Biochimica Polonica

2005

tom 52

nr 3

In line with our studies on propafenone-type inhibitors of P-glycoprotein (P-gp), we applied several methods to approach virtual screening tools for identification of new P-gp inhibitors on one hand and the molecular basis of ligand-protein interaction on the other hand. For virtual screening, a combination of autocorrelation vectors and selforganising artificial neural networks proved extremely valuable in identifying P-gp inhibitors with structurally new scaffolds. For a closer view on the binding region for propafenone-type ligands we applied a combination of pharmacophore-driven photoaffinity labeling and protein homology modeling. On LmrA, a bacterial homologue of P-gp, we were able to identify distinct regions on transmembrane helices 3, 5 and 6 which show significant changes in the labeling pattern during different steps of the catalytic cycle.