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2. Characterization of benzodiazepine binding site on human alpha1-acid glycoprotein using flunitrazepam as a photolabeling agent

Author

Teppei Hara, Ken-ichi Kaneko, Motoki Hijioka, Masaki Otagiri, Koji Nishi, Victor Tuan Giam Chuang, Akihiko Kuniyasu, Masaaki Katsuki, Megumi Ueno, and Hitoshi Nakayama

Subjects
Sequence analysis, Molecular Sequence Data, Biophysics, Asialoglycoproteins, Peptide, Flunitrazepam, Photoaffinity Labels, Biochemistry, chemistry.chemical_compound, medicine, Humans, Trypsin, Amino Acid Sequence, Cyanogen Bromide, Molecular Biology, chemistry.chemical_classification, Binding Sites, Genetic Variation, Orosomucoid, Peptide Fragments, Sialic acid, chemistry, Covalent bond, Benzodiazepine binding, α1 acid glycoprotein, Glycoprotein, medicine.drug
Abstract

The binding of flunitrazepam (FNZP) by human α1-acid glycoprotein (hAGP) and the relationships between the extent of drug binding and desialylation and the genetic variants of hAGP were examined. The photolabeling specificity of [3H]FNZP was confirmed by findings in which other hAGP-binding ligands inhibited the formation of covalent bonds between [3H]FNZP and hAGP. The photolabeling of asialo-hAGP suggested that sialic acid does not involve in the binding of [3H]FNZP. No difference in the labeling could be found between the F1 * S variants and A variant. Similarly, FNZP did not show a difference in binding affinity to the two genetic variants of hAGP. Sequence analysis of the photolabeled peptide indicated a sequence corresponding to Tyr91-Arg105 of hAGP.

Published
2005

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