Hydrophobic binding of phenoxyacetic and phenylacetic acids to horseradish peroxidase and human serum albumin: structure-activity relationships.
Studies of protein binding in homologous series of drugs are of great interest for drug research. Apparent binding constants of phenoxyacetic and phenylacetic acids to horseradish peroxidase and to human serum albumin are evaluated by NMR studies and an optical method. These constants are good parameters to describe hydrophobic interactions, and the results are in a good agreement with our protein binding model described previously.
D055598:Chemical Phenomena; D002621:Chemistry; D006016:Glycolates / Q000378:metabolism*; D006735:Horseradish Peroxidase / Q000378:metabolism*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D010544:Peroxidases / Q000378:metabolism*; D010642:Phenoxyacetates / Q000378:metabolism*; D010648:Phenylacetates / Q000378:metabolism*; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D013329:Structure-Activity Relationship
D006016:Glycolates; D010642:Phenoxyacetates; D010648:Phenylacetates; D012709:Serum Albumin; D006735:Horseradish Peroxidase; D010544:Peroxidases