19F-n.m.r. study of trifluoperazine-S100 protein interaction: effects of Ca2+ and Zn2+.
19F-n.m.r. spectra were measured to investigate the effects of Ca2+ and Zn2+ on the interaction of trifluoperazine (TFP) with three S100 proteins. It was found that TFP binds to S100a and S100ao proteins irrespective of the presence of Ca2+ and Zn2+, while in the presence of Ca2+ the apparent affinity of TFP to the proteins was greater than that in its absence or in the presence of Zn2+. In contrast, the binding affinity of TRP to S100b protein in the presence and absence of metal ions was lower than to S100a and S100ao proteins. These results suggested that TFP binds to each S100 protein in two ways: one is Ca2(+)- or Zn2(+)-dependent specific manner and another is Ca2(+)- or Zn2(+)-independent non-specific manner.
Ogoma
Y
Y
Department of Functional Polymer Science, Faculty of Textile Science and Technology, Shinshu, University, Ueda, Japan.
Kobayashi
H
H
Fujii
T
T
Kondo
Y
Y
Hachimori
A
A
Shimizu
T
T
Hatano
M
M
D002118:Calcium / Q000494:pharmacology*; D009682:Magnetic Resonance Spectroscopy; D009418:S100 Proteins / Q000737:chemistry*; D014268:Trifluoperazine / Q000737:chemistry*; D015032:Zinc / Q000494:pharmacology*
D009418:S100 Proteins; D014268:Trifluoperazine; D015032:Zinc; D002118:Calcium