Collagen glycation detected by its intrinsic fluorescence

Rhona Muir, Shareen Forbes, David J.S. Birch, Vladislav Vyshemirsky, Olaf J. Rolinski

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)
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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.
Original languageEnglish
Pages (from-to)11058–11066
Number of pages9
JournalJournal of Physical Chemistry B
Issue number39
Early online date24 Sept 2021
Publication statusPublished - 7 Oct 2021


  • materials chemistry
  • surfaces, coatings and films
  • physical and theoretical chemistry


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