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

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 p...

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Bibliographic Details
Published in:Phytochemistry (Oxford) 1999-08, Vol.51 (7), p.867-872
Main Authors: Feldman, K.S., Sambandam, A., Lemon, S.T., Nicewonger, R.B., Long, G.S., Battaglia, D.F., Ensel, S.M., Laci, M.A.
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Equilibrium dialysis
Flavonoids
Fundamental and applied biological sciences. Psychology
Gallotannin
Hydrolyzable Tannins - metabolism
Intermediary metabolites. Miscellaneous
Magnetic Resonance Spectroscopy
Molecular Structure
Other biological molecules
Phenols - metabolism
Polymers - metabolism
Polyphenols
Protein Binding
Serum Albumin, Bovine - metabolism
Spectrometry, Mass, Fast Atom Bombardment
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Summary: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.
ISSN:0031-9422
1873-3700
DOI:10.1016/S0031-9422(99)00144-2