Binding affinities of gallotannin analogs with bovine serum albumin: ramifications for polyphenol-protein molecular recognition.

@article{Feldman1999BindingAO,
  title={Binding affinities of gallotannin analogs with bovine serum albumin: ramifications for polyphenol-protein molecular recognition.},
  author={Ken S. Feldman and Aruna Sambandam and Stephen Lemon and Robert B Nicewonger and Gregory S Long and Deborah F Battaglia and S M Ensel and M A Laci},
  journal={Phytochemistry},
  year={1999},
  volume={51 7},
  pages={867-72}
}
A series of gallotannin analogs were prepared by chemical synthesis, and their affinity for the test-case protein bovine serum albumin was measured by equilibrium dialysis. The structure/activity data obtained suggest that the naturally occurring gallotannins, in fact, do not represent the optimal protein recognition agents amongst polyphenolated templates.