Chiral discrimination of N-carbazole-carbonyl derivatives of α-amino acids with a short linear alkyl side chain by bovine serum albumin

Yoshihiro Abe, Tomoko Shoji, Mamiko Matsubara, Midori Yoshida, Setsuro Sugata, Kazunori Iwata, Hiroshi Suzuki

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Chiral discrimination of racemic carbazole carbonyl (CC)-amino acids with linear alkyl sidechain (C1-C4) by bovine serum albumin (BSA) was investigated by competitive replacement experiments using dansyl-L-proline and dansyl-D-norvaline as fluorescent probes. It was found that the CC derivatives of the D-forms of alanine (C1), amino butyric acid (C2), norvaline (C3), and norleucine (C4) bound to the dansyl-L-proline site much more strongly than their L-forms, whereas the interactions between both enantiomers of these amino acids with dansyl-D-norvaline site were slight. (C) 2000 Wiley-Liss, Inc.

Original languageEnglish
Pages (from-to)565-567
Number of pages3
JournalChirality
Volume12
Issue number7
DOIs
Publication statusPublished - 2000 Jan 1

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Keywords

  • Bovine serum albumin
  • Carbazole-carbonyl amino acids
  • Chiral discrimination
  • Enantioseparation
  • HPLC

ASJC Scopus subject areas

  • Analytical Chemistry
  • Catalysis
  • Pharmacology
  • Drug Discovery
  • Spectroscopy
  • Organic Chemistry

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