Probe molecule equipped with boronic acid moiety as a reversible cross-linking group improves its binding affinity.
Syntheses of biotinylated probe molecules of L-glutathione (GSH) equipped with boronic acid moiety and evaluation of their binding affinities against glutathione-S-transferase (GST) were described. It revealed that the presence of boronic acid moiety in an appropriate position enhances binding affinity of GSH probe toward GST probably by forming a reversible cross-link. Among prepared, the boronate-containing probe 8b exhibited the highest recovering ability of GST from Escherichia coli cell lysate.
Graduate School of Pharmaceutical Sciences, Osaka University, 1-6 Yamada-oka, Suita, Osaka 565-0871, Japan.
Naoyuki
N
Kotoku
Xiu-Han
XH
Guo
Masayoshi
M
Arai
Motomasa
M
Kobayashi
D001897:Boronic Acids / Q000737:chemistry* / Q000378:metabolism; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D005978:Glutathione / Q000737:chemistry / Q000378:metabolism*; D005982:Glutathione Transferase / Q000378:metabolism; D015335:Molecular Probes; D013379:Substrate Specificity
D001897:Boronic Acids; D015335:Molecular Probes; D005982:Glutathione Transferase; D005978:Glutathione