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

K S Feldman; A Sambandam; S T Lemon; R B Nicewonger; G S Long; D F Battaglia; S M Ensel; M A Laci

doi:10.1016/s0031-9422(99)00144-2

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

Phytochemistry. 1999 Aug;51(7):867-72. doi: 10.1016/s0031-9422(99)00144-2.

Authors

K S Feldman¹, A Sambandam, S T Lemon, R B Nicewonger, G S Long, D F Battaglia, S M Ensel, M A Laci

Affiliation

¹ Department of Chemistry, Pennsylvania State University, University Park 16802, USA.

PMID: 10423859
DOI: 10.1016/s0031-9422(99)00144-2

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

Research Support, U.S. Gov't, P.H.S.

MeSH terms

Flavonoids*
Hydrolyzable Tannins / metabolism*
Magnetic Resonance Spectroscopy
Molecular Structure
Phenols / metabolism*
Polymers / metabolism*
Polyphenols
Protein Binding
Serum Albumin, Bovine / metabolism*
Spectrometry, Mass, Fast Atom Bombardment

Substances

Flavonoids
Hydrolyzable Tannins
Phenols
Polymers
Polyphenols
Serum Albumin, Bovine

Grants and funding

GM35727/GM/NIGMS NIH HHS/United States