Abstract
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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Flavonoids*
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Hydrolyzable Tannins / metabolism*
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Magnetic Resonance Spectroscopy
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Molecular Structure
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Phenols / metabolism*
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Polymers / metabolism*
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Polyphenols
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Protein Binding
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Serum Albumin, Bovine / metabolism*
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Spectrometry, Mass, Fast Atom Bombardment
Substances
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Flavonoids
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Hydrolyzable Tannins
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Phenols
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Polymers
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Polyphenols
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Serum Albumin, Bovine