Transthyretin Binding Heterogeneity and Anti-amyloidogenic Activity of Natural Polyphenols and Their Metabolites.

@article{Florio2015TransthyretinBH,
  title={Transthyretin Binding Heterogeneity and Anti-amyloidogenic Activity of Natural Polyphenols and Their Metabolites.},
  author={Paola Florio and Claudia Folli and Michele Cianci and Daniele Del Rio and Giuseppe Zanotti and Rodolfo Berni},
  journal={The Journal of biological chemistry},
  year={2015},
  volume={290 50},
  pages={29769-80}
}
Transthyretin (TTR) is an amyloidogenic protein, the amyloidogenic potential of which is enhanced by a number of specific point mutations. The ability to inhibit TTR fibrillogenesis is known for several classes of compounds, including natural polyphenols, which protect the native state of TTR by specifically interacting with its thyroxine binding sites. Comparative analyses of the interaction and of the ability to protect the TTR native state for polyphenols, both stilbenoids and flavonoids… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.

Similar Papers

Loading similar papers…