title: 1H and 13C NMR study of the molecular interaction mechanism between chloramphenicol and human serum albumin.
abstract: Molecular mechanism of the interaction between human serum albumin and cloramphenicol was studied by 1H and 13C NMR-spectroscopy. It was found that the main role belongs to [formula: see text] groups of chloramphenicol. A schematic model of the complex-formation between serum albumin and chloramphenicol was proposed.
authors.affiliation: Institute of Chemical Physics RAS, Moscow, Russia.
authors.forename: V
authors.initials: V
authors.lastname: Panov
authors.forename: I
authors.initials: I
authors.lastname: Shipanova
authors.forename: A
authors.initials: A
authors.lastname: Michtchenko
authors.forename: I
authors.initials: I
authors.lastname: Shabunin
authors.forename: N
authors.initials: N
authors.lastname: Shimanovskii
authors.forename: L
authors.initials: L
authors.lastname: Sibeldina
authors.forename: P
authors.initials: P
authors.lastname: Sergeev
mesh_terms: D001665:Binding Sites; D002247:Carbon Isotopes; D002701:Chloramphenicol / Q000378:metabolism*; D006801:Humans; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008961:Models, Structural; D011485:Protein Binding; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D002247:Carbon Isotopes; D012709:Serum Albumin; D002701:Chloramphenicol; D006859:Hydrogen