title: Ligand binding to domain-3 of human serum albumin: a chemometric analysis.
abstract: A detailed chemometric analysis of ligand binding to domain-3A of human serum albumin is described. NMR and fluorescence data on a set of 889 chemically diverse compounds were used to develop a group contribution model based on 74 chemical fragments that is in good agreement with the experimental data (R2 = 0.94, Q2 = 0.90). The structural descriptors used in this analysis comprise a convenient look-up table for quantitatively estimating the effect that a particular group will have on albumin binding. This information can be valuable for optimizing a particular series of compounds for drug development.
mesh_terms: D001665:Binding Sites; D015195:Drug Design; D006801:Humans; D008024:Ligands; D008956:Models, Chemical; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D021281:Quantitative Structure-Activity Relationship; D012709:Serum Albumin / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence
chemical_list: D008024:Ligands; D010446:Peptide Fragments; D012709:Serum Albumin