Transition Metal Ion Binding Studies of Carnosine and Histidine: Biologically Relevant Antioxidants

Stephanie Velez; Nanditha G. Nair; Prakash Reddy

doi:10.1016/j.colsurfb.2008.06.012

Transition Metal Ion Binding Studies of Carnosine and Histidine: Biologically Relevant Antioxidants

Stephanie Velez
, Nanditha G. Nair
, Prakash Reddy

Missouri University of Science and Technology

Research output: Contribution to journal › Article › peer-review

Abstract

Carnosine and histidine are biologically interesting antioxidants. In order to probe whether they exert their antioxidant effect through metal ion chelation, the Cu(II) ion chelating abilities of these compounds were measured by UV-vis spectroscopy. Both of these compounds showed 1:1 complexations with Cu(II) ions as shown by their Job's plot. The binding constants for histidine and carnosine, as determined by Benesi-Hildebrand method, at pH 7.84 ± 0.18, were found to be 71 and 1.1 M ^-1 , respectively. The unexpectedly lower binding constant values of carnosine show the relatively minor role of the transition metal ion chelation in their antioxidant abilities.

Original language	American English
Journal	Colloids and Surfaces B: Biointerfaces
Volume	66
DOIs	https://doi.org/10.1016/j.colsurfb.2008.06.012
State	Published - Oct 1 2008

Keywords

Antioxidant
Antioxidant effect
Arsenic compounds
Benesi-Hildebrand
Binding Sites
Binding constants
Binding, Competitive
Carnosine
Chelation
Chlorine compounds
Complexation
Copper alloys
Cu (II)
Histidine
Hydrogen-Ion Concentration
Ions
Job's plot
Metal ion binding
Metal ions
Metals
Molecular Structure
Spectrophotometry, Ultraviolet
Surface Properties
Transition metal compounds
Transition metals
Transition-metal ions
UV-VIS spectroscopy
Ultraviolet spectroscopy
binding affinity
chelating agent
chelation
complex formation
copper ion
methodology
pH
priority journal

Disciplines

Chemistry

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title = "Transition Metal Ion Binding Studies of Carnosine and Histidine: Biologically Relevant Antioxidants",

abstract = " Carnosine and histidine are biologically interesting antioxidants. In order to probe whether they exert their antioxidant effect through metal ion chelation, the Cu(II) ion chelating abilities of these compounds were measured by UV-vis spectroscopy. Both of these compounds showed 1:1 complexations with Cu(II) ions as shown by their Job's plot. The binding constants for histidine and carnosine, as determined by Benesi-Hildebrand method, at pH 7.84 ± 0.18, were found to be 71 and 1.1 M -1 , respectively. The unexpectedly lower binding constant values of carnosine show the relatively minor role of the transition metal ion chelation in their antioxidant abilities.",

keywords = "Antioxidant, Antioxidant effect, Arsenic compounds, Benesi-Hildebrand, Binding Sites, Binding constants, Binding, Competitive, Carnosine, Chelation, Chlorine compounds, Complexation, Copper alloys, Cu (II), Histidine, Hydrogen-Ion Concentration, Ions, Job's plot, Metal ion binding, Metal ions, Metals, Molecular Structure, Spectrophotometry, Ultraviolet, Surface Properties, Transition metal compounds, Transition metals, Transition-metal ions, UV-VIS spectroscopy, Ultraviolet spectroscopy, binding affinity, chelating agent, chelation, complex formation, copper ion, methodology, pH, priority journal",

author = "Stephanie Velez and Nair, \{Nanditha G.\} and Prakash Reddy",

year = "2008",

month = oct,

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doi = "10.1016/j.colsurfb.2008.06.012",

language = "American English",

volume = "66",

journal = "Colloids and Surfaces B: Biointerfaces",

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T1 - Transition Metal Ion Binding Studies of Carnosine and Histidine: Biologically Relevant Antioxidants

AU - Velez, Stephanie

AU - Nair, Nanditha G.

AU - Reddy, Prakash

PY - 2008/10/1

Y1 - 2008/10/1

N2 - Carnosine and histidine are biologically interesting antioxidants. In order to probe whether they exert their antioxidant effect through metal ion chelation, the Cu(II) ion chelating abilities of these compounds were measured by UV-vis spectroscopy. Both of these compounds showed 1:1 complexations with Cu(II) ions as shown by their Job's plot. The binding constants for histidine and carnosine, as determined by Benesi-Hildebrand method, at pH 7.84 ± 0.18, were found to be 71 and 1.1 M -1 , respectively. The unexpectedly lower binding constant values of carnosine show the relatively minor role of the transition metal ion chelation in their antioxidant abilities.

AB - Carnosine and histidine are biologically interesting antioxidants. In order to probe whether they exert their antioxidant effect through metal ion chelation, the Cu(II) ion chelating abilities of these compounds were measured by UV-vis spectroscopy. Both of these compounds showed 1:1 complexations with Cu(II) ions as shown by their Job's plot. The binding constants for histidine and carnosine, as determined by Benesi-Hildebrand method, at pH 7.84 ± 0.18, were found to be 71 and 1.1 M -1 , respectively. The unexpectedly lower binding constant values of carnosine show the relatively minor role of the transition metal ion chelation in their antioxidant abilities.

KW - Antioxidant

KW - Antioxidant effect

KW - Arsenic compounds

KW - Benesi-Hildebrand

KW - Binding Sites

KW - Binding constants

KW - Binding, Competitive

KW - Carnosine

KW - Chelation

KW - Chlorine compounds

KW - Complexation

KW - Copper alloys

KW - Cu (II)

KW - Histidine

KW - Hydrogen-Ion Concentration

KW - Ions

KW - Job's plot

KW - Metal ion binding

KW - Metal ions

KW - Metals

KW - Molecular Structure

KW - Spectrophotometry, Ultraviolet

KW - Surface Properties

KW - Transition metal compounds

KW - Transition metals

KW - Transition-metal ions

KW - UV-VIS spectroscopy

KW - Ultraviolet spectroscopy

KW - binding affinity

KW - chelating agent

KW - chelation

KW - complex formation

KW - copper ion

KW - methodology

KW - pH

KW - priority journal

UR - https://scholarsmine.mst.edu/chem_facwork/181

UR - https://doi.org/10.1016/j.colsurfb.2008.06.012

U2 - 10.1016/j.colsurfb.2008.06.012

DO - 10.1016/j.colsurfb.2008.06.012

M3 - Article

SN - 1873-4367

VL - 66

JO - Colloids and Surfaces B: Biointerfaces

JF - Colloids and Surfaces B: Biointerfaces

ER -

Transition Metal Ion Binding Studies of Carnosine and Histidine: Biologically Relevant Antioxidants

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