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

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

Chemistry

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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.

Original language	English (US)
Pages (from-to)	867-872
Number of pages	6
Journal	Phytochemistry
Volume	51
Issue number	7
DOIs	https://doi.org/10.1016/S0031-9422(99)00144-2
State	Published - Aug 1999

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Plant Science
Horticulture

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10.1016/S0031-9422(99)00144-2

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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.",

author = "Feldman, {K. S.} and A. Sambandam and Lemon, {S. T.} and Nicewonger, {R. B.} and Long, {G. S.} and Battaglia, {D. F.} and Ensel, {S. M.} and Laci, {M. A.}",

note = "Funding Information: We thank the National Institutes of Health (GM35727) for support of this work. ",

year = "1999",

month = aug,

doi = "10.1016/S0031-9422(99)00144-2",

language = "English (US)",

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journal = "Phytochemistry",

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T1 - Binding affinities of gallotannin analogs with bovine serum albumin

T2 - Ramifications for polyphenol-protein molecular recognition

AU - Feldman, K. S.

AU - Sambandam, A.

AU - Lemon, S. T.

AU - Nicewonger, R. B.

AU - Long, G. S.

AU - Battaglia, D. F.

AU - Ensel, S. M.

AU - Laci, M. A.

N1 - Funding Information: We thank the National Institutes of Health (GM35727) for support of this work.

PY - 1999/8

Y1 - 1999/8

N2 - 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.

AB - 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.

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U2 - 10.1016/S0031-9422(99)00144-2

DO - 10.1016/S0031-9422(99)00144-2

M3 - Article

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AN - SCOPUS:0033181085

SN - 0031-9422

VL - 51

SP - 867

EP - 872

JO - Phytochemistry

JF - Phytochemistry

IS - 7

ER -

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

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