title: Binding affinities of gallotannin analogs with bovine serum albumin: ramifications for polyphenol-protein molecular recognition.
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.
authors.affiliation: Department of Chemistry, Pennsylvania State University, University Park 16802, USA.
authors.forename: K S
authors.initials: KS
authors.lastname: Feldman
authors.forename: A
authors.initials: A
authors.lastname: Sambandam
authors.forename: S T
authors.initials: ST
authors.lastname: Lemon
authors.forename: R B
authors.initials: RB
authors.lastname: Nicewonger
authors.forename: G S
authors.initials: GS
authors.lastname: Long
authors.forename: D F
authors.initials: DF
authors.lastname: Battaglia
authors.forename: S M
authors.initials: SM
authors.lastname: Ensel
authors.forename: M A
authors.initials: MA
authors.lastname: Laci
mesh_terms: 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
chemical_list: D005419:Flavonoids; D047348:Hydrolyzable Tannins; D010636:Phenols; D011108:Polymers; D059808:Polyphenols; D012710:Serum Albumin, Bovine