Interaction of trifluoperazine with S100 protein: a 19F NMR study
1987; Elsevier BV; Volume: 138; Issue: 2 Linguagem: Inglês
10.1016/s0020-1693(00)81198-6
ISSN1873-3255
AutoresYoshiro Ogoma, Tetsuya Miwa, Toshihiro Fujii, Yoshiyuki Kondo, Akira Hachimori, Tôru Shimizu, Masahiro Hatano,
Tópico(s)Machine Learning in Bioinformatics
Resumo19F NMR spectra were measured to investigate the interaction of trifluoperazine (TFP) with porcine brain S100 protein (S100) under various conditions. It was found that TFP binds to S100 irrespective of Ca2+. However, in the presence of Ca2+ the apparent affinity of TFP to protein (Kd = 20 μM) was greater than that in its absence (Kd = 85 μM). Zn2+ also enhanced the binding of TFP to S100. The ratio of TFP bound to S100 was estimated to be nearly unity in the presence of Ca2+. It was also found that KCl only markedly affected the interaction of TFP with S100 in the presence of Ca2+. The 19F NMR chemical shift of the TFP-S100 solution changed much depending upon the pH of the solution in the presence of Ca2+, while no remarkable pH dependence of the 19F NMR chemical shift was observed for the TFP-S100 solution in the absence of Ca2+. These pH effects are in contrast wih those observed for the TFP-calmodulin solution.
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