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NMR spectroscopic diffusion, chemical shift and linewidth measurements of low‐affinity binding of ibuprofen enantiomers to human serum albumin
Author(s) -
Ma Yuehong,
Liu Maili,
Mao Xian,
Nicholson Jeremy K.,
Lindon John C.
Publication year - 1999
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/(sici)1097-458x(199904)37:4<269::aid-mrc446>3.0.co;2-u
Subject(s) - chemistry , human serum albumin , enantiomer , diffusion , nuclear magnetic resonance spectroscopy , molecule , serum albumin , binding site , stereochemistry , organic chemistry , chromatography , biochemistry , thermodynamics , physics
The binding of racemic, ( R )(−) and ( S )(+)‐ibuprofen (IBP) to humanserum albumin (HSA) was studied using NMR spectroscopy.Having saturated the tight binding sites, the extent of weak bindingwas then investigated. The molecular diffusion coefficients of IBP inHSA solution at different concentration ratios indicate that there isno significant difference in binding capacity of the two enantiomersof IBP to HSA at high IBP: HSA ratios. However, there are chemicalshift and linewidth changes in the 1 NMR spectrum of IBP inthe presence of HSA induced by the binding and this suggests that themajor binding interaction involves the sec ‐butyl chainof the IBP molecule binding to HSA in hydrophobic pockets. Copyright© 1999 John Wiley & Sons, Ltd.