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Collagen Glycation Detected by Its Intrinsic Fluorescence.

ABSTRACT: Collagen's long half-life (in skin approximately 10 years) makes this protein highly susceptible to glycation and formation of the advanced glycation end products (AGEs). Accumulation of cross-linking AGEs in the skin collagen has several detrimental effects; thus, the opportunity for non-invasive monitoring of skin glycation is essential, especially for diabetic patients. In this paper, we report using the time-resolved intrinsic fluorescence of collagen as a biomarker of its glycation. Contrary to the traditional fluorescence intensity decay measurement at the arbitrarily selected excitation and detection wavelengths, we conducted systematic wavelength- and time-resolved measurements to achieve time-resolved emission spectra. Changes in the intrinsic fluorescence kinetics, caused by both collagen aggregation and glycation, have been detected.

SUBMITTER: Muir R

PROVIDER: S-EPMC8793138 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature

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Collagen Glycation Detected by Its Intrinsic Fluorescence.

Muir Rhona R Forbes Shareen S Birch David J S DJS Vyshemirsky Vladislav V Rolinski Olaf J OJ

The journal of physical chemistry. B 20210924 39

Collagen's long half-life (in skin approximately 10 years) makes this protein highly susceptible to glycation and formation of the advanced glycation end products (AGEs). Accumulation of cross-linking AGEs in the skin collagen has several detrimental effects; thus, the opportunity for non-invasive monitoring of skin glycation is essential, especially for diabetic patients. In this paper, we report using the time-resolved intrinsic fluorescence of collagen as a biomarker of its glycation. Contrar ...[more]

PMID: 34555903

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