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Reversible binding interactions between the tryptophan enantiomers and albumins of different animal species as determined by novel high performance liquid chromatographic methods: an attempt to localize the D‐ and L‐tryptophan binding sites on the human serum albumin polypeptide chain by using protein fragments
Author(s) -
Šoltés Ladislav,
Sebille Bernard
Publication year - 1997
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/(sici)1520-636x(1997)9:4<373::aid-chir10>3.0.co;2-k
Subject(s) - chemistry , enantiomer , tryptophan , chromatography , high performance liquid chromatography , human serum albumin , bovine serum albumin , sorbent , albumin , amino acid , organic chemistry , biochemistry , adsorption
The stereoselectivity of the reversible binding interactions between the D‐ and L‐tryptophan enantiomers and serum albumins of different animal species and fragments of human serum albumin (HSA) was investigated by applying three novel high performance liquid chromatographic (HPLC) arrangements. The separations were performed by means of (1) an achiral (diol‐bond), (2) a chiral (bovine serum albumin‐bond) silica gel sorbent, and (3) a column switching technique which uses both the diol‐ and HSA‐bond HPLC stationary phases. A polarimetric detector and/or an ultraviolet (UV) spectrophotometer were used to monitor the separation process. HPLC arrangement 3 allowed the evaluation of enantioselective binding for D‐ and L‐tryptophan to different albumins and albumin fragments. At present, column switching can be considered the technique of the broadest applicability for investigating the reversible binding interactions between a protein and drug enantiomers. Chirality 9:373–379, 1997. © 1997 Wiley‐Liss, Inc.