Collagen glycation detected by its intrinsic fluorescence

Muir, R., Forbes, S., Birch, D. J.S., Vyshemirsky, V. and Rolinski, O. J. (2021) Collagen glycation detected by its intrinsic fluorescence. Journal of Physical Chemistry B, 125(39), pp. 11058-11066. (doi: 10.1021/acs.jpcb.1c05001) (PMID:34555903)

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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.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Vyshemirsky, Dr Vladislav
Authors: Muir, R., Forbes, S., Birch, D. J.S., Vyshemirsky, V., and Rolinski, O. J.
College/School:College of Science and Engineering > School of Mathematics and Statistics > Statistics
Journal Name:Journal of Physical Chemistry B
Publisher:American Chemical Society
ISSN (Online):1520-5207
Published Online:24 September 2021

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