Collagen glycation detected by its intrinsic fluorescence
Muir, Rhona and Forbes, Shareen and Birch, David J.S. and Vyshemirsky, Vladislav and Rolinski, Olaf J. (2021) Collagen glycation detected by its intrinsic fluorescence. Journal of Physical Chemistry B, 125 (39). 11058–11066. ISSN 1520-6106 (https://doi.org/10.1021/acs.jpcb.1c05001)
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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.
ORCID iDs
Muir, Rhona, Forbes, Shareen, Birch, David J.S. ORCID: https://orcid.org/0000-0001-6400-1270, Vyshemirsky, Vladislav and Rolinski, Olaf J. ORCID: https://orcid.org/0000-0002-7838-779X;-
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Item type: Article ID code: 79400 Dates: DateEvent7 October 2021Published24 September 2021Published Online24 September 2021AcceptedSubjects: Science > Chemistry Department: Faculty of Science > Physics
Faculty of Science > Mathematics and StatisticsDepositing user: Pure Administrator Date deposited: 01 Feb 2022 15:04 Last modified: 08 Oct 2024 00:22 URI: https://strathprints.strath.ac.uk/id/eprint/79400