Evaluating the Reduced Hydrophobic Taste Sensor Response of Dipeptides by Theasinensin A by Using NMR and Quantum Mechanical Analyses

@article{Guo2016EvaluatingTR,
  title={Evaluating the Reduced Hydrophobic Taste Sensor Response of Dipeptides by Theasinensin A by Using NMR and Quantum Mechanical Analyses},
  author={J. Guo and N. Hirasaki and Y. Miyata and Kazunari Tanaka and Takashi Tanaka and Xiao Wu and Y. Tahara and K. Toko and T. Matsui},
  journal={PLoS ONE},
  year={2016},
  volume={11}
}
The current study demonstrated that theasinensin A (TSA) had a potential to form the complex with hydrophobic Trp-containing dipeptides, and to reduce their membrane potential by artificial-lipid membrane taste sensor. At a 1:3 molar ratio of the 6 Trp-containing dipeptides together with TSA, we observed a significant chemical shift of the protons of the dipeptides (Δδ) to a high magnetic field, when analyzed using 1H-nuclear-magnetic resonance (NMR) spectroscopy. The Δδ values were correlated… Expand

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