1H and 13C NMR study of the molecular interaction mechanism between chloramphenicol and human serum albumin.
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.
Panov
V
V
Institute of Chemical Physics RAS, Moscow, Russia.
Shipanova
I
I
Michtchenko
A
A
Shabunin
I
I
Shimanovskii
N
N
Sibeldina
L
L
Sergeev
P
P
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*
D002247:Carbon Isotopes; D012709:Serum Albumin; D002701:Chloramphenicol; D006859:Hydrogen