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 protein recognition agents amongst polyphenolated templates.
Feldman
K S
KS
Department of Chemistry, Pennsylvania State University, University Park 16802, USA.
Sambandam
A
A
Lemon
S T
ST
Nicewonger
R B
RB
Long
G S
GS
Battaglia
D F
DF
Ensel
S M
SM
Laci
M A
MA
D005419:Flavonoids; D047348:Hydrolyzable Tannins / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D010636:Phenols / Q000378:metabolism*; D011108:Polymers / Q000378:metabolism*; D059808:Polyphenols; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D016339:Spectrometry, Mass, Fast Atom Bombardment
D005419:Flavonoids; D047348:Hydrolyzable Tannins; D010636:Phenols; D011108:Polymers; D059808:Polyphenols; D012710:Serum Albumin, Bovine