Paclitaxel binding to the fatty acid-induced conformation of human serum albumin--automated docking studies.

Paclitaxel (Taxol((R))) binding to the conformation of human serum albumin assumed in the presence of long-chain fatty acids was studied by automated docking. Reduced binding affinities at both the primary and secondary sites were predicted, compared to those characterizing the interaction with the fatty acid-free protein. The baccatin core of paclitaxel was found to play a more important role than its C13 side chain in determining the ligand binding mode as well as in contributing to the overall binding energy at the primary site.