Physicochemical studies on the copper(II) binding by glycated collagen telopeptides.

Meder Kamalov; Paul W R Harris; Christian G Hartinger; Gordon M Miskelly; Garth J S Cooper; Margaret A Brimble

doi:10.1039/c4ob02536a

Physicochemical studies on the copper(II) binding by glycated collagen telopeptides.

Meder Kamalov, Paul W R Harris, Christian G Hartinger, Gordon M Miskelly, Garth J S Cooper, Margaret A Brimble

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

Abstract

Emerging evidence indicates that levels of advanced glycation end-products (AGEs) correlate with age- and diabetes-related organ damage and may play a causative role in such damage. Increased chelation of Cu(II) ions appears to play an important role in this process, however, the precise relationship between formation of AGEs and accumulation of Cu(II) is yet to be determined. The interaction between AGEs and Cu(II) has been investigated using a collagenous peptide that has been site-specifically modified by a key AGE. Potentiometric titration showed that introduction of this AGE increased the capacity of the host-peptide to bind Cu(II). This result was confirmed by mass spectrometric characterisation of the AGE-modified peptide-Cu(II) system.

Original language	English
Journal	Organic & biomolecular chemistry
Volume	13
Issue number	10
DOIs	https://doi.org/10.1039/c4ob02536a
Publication status	Published - 14 Mar 2015

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10.1039/c4ob02536a

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abstract = "Emerging evidence indicates that levels of advanced glycation end-products (AGEs) correlate with age- and diabetes-related organ damage and may play a causative role in such damage. Increased chelation of Cu(II) ions appears to play an important role in this process, however, the precise relationship between formation of AGEs and accumulation of Cu(II) is yet to be determined. The interaction between AGEs and Cu(II) has been investigated using a collagenous peptide that has been site-specifically modified by a key AGE. Potentiometric titration showed that introduction of this AGE increased the capacity of the host-peptide to bind Cu(II). This result was confirmed by mass spectrometric characterisation of the AGE-modified peptide-Cu(II) system.",

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AU - Harris, Paul W R

AU - Hartinger, Christian G

AU - Miskelly, Gordon M

AU - Cooper, Garth J S

AU - Brimble, Margaret A

PY - 2015/3/14

Y1 - 2015/3/14

N2 - Emerging evidence indicates that levels of advanced glycation end-products (AGEs) correlate with age- and diabetes-related organ damage and may play a causative role in such damage. Increased chelation of Cu(II) ions appears to play an important role in this process, however, the precise relationship between formation of AGEs and accumulation of Cu(II) is yet to be determined. The interaction between AGEs and Cu(II) has been investigated using a collagenous peptide that has been site-specifically modified by a key AGE. Potentiometric titration showed that introduction of this AGE increased the capacity of the host-peptide to bind Cu(II). This result was confirmed by mass spectrometric characterisation of the AGE-modified peptide-Cu(II) system.

AB - Emerging evidence indicates that levels of advanced glycation end-products (AGEs) correlate with age- and diabetes-related organ damage and may play a causative role in such damage. Increased chelation of Cu(II) ions appears to play an important role in this process, however, the precise relationship between formation of AGEs and accumulation of Cu(II) is yet to be determined. The interaction between AGEs and Cu(II) has been investigated using a collagenous peptide that has been site-specifically modified by a key AGE. Potentiometric titration showed that introduction of this AGE increased the capacity of the host-peptide to bind Cu(II). This result was confirmed by mass spectrometric characterisation of the AGE-modified peptide-Cu(II) system.

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SN - 1477-0539

VL - 13

JO - Organic & biomolecular chemistry

JF - Organic & biomolecular chemistry

IS - 10

ER -

Physicochemical studies on the copper(II) binding by glycated collagen telopeptides.

Abstract

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