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.
Paal
Krisztina
K
Faculty of Science, University of Ontario Institute of Technology, 2000 Simcoe Street North, Oshawa, Ont., Canada.
Shkarupin
Aliaksei
A
D000970:Antineoplastic Agents / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D003198:Computer Simulation; D000077143:Docetaxel; D005227:Fatty Acids / Q000737:chemistry*; D006801:Humans; D006860:Hydrogen Bonding; D008024:Ligands; D008958:Models, Molecular; D015394:Molecular Structure; D017239:Paclitaxel / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D012709:Serum Albumin / Q000378:metabolism*; D043823:Taxoids / Q000737:chemistry / Q000378:metabolism
D000970:Antineoplastic Agents; D005227:Fatty Acids; D008024:Ligands; D012709:Serum Albumin; D043823:Taxoids; D000077143:Docetaxel; D017239:Paclitaxel