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Quansah, Elsie; Shaik, Tanveer Ahmed; Çevik, Ecehan; Wang, Xinyue; Höppener, Christiane; Meyer-Zedler, Tobias; Deckert, Volker; Schmitt, Michael; Popp, Jürgen; Krafft, Christoph

Investigating biochemical and structural changes of glycated collagen using multimodal multiphoton imaging, Raman spectroscopy, and atomic force microscopy

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  • Media type: E-Article
  • Title: Investigating biochemical and structural changes of glycated collagen using multimodal multiphoton imaging, Raman spectroscopy, and atomic force microscopy
  • Contributor: Quansah, Elsie; Shaik, Tanveer Ahmed; Çevik, Ecehan; Wang, Xinyue; Höppener, Christiane; Meyer-Zedler, Tobias; Deckert, Volker; Schmitt, Michael; Popp, Jürgen; Krafft, Christoph
  • imprint: Springer Science and Business Media LLC, 2023
  • Published in: Analytical and Bioanalytical Chemistry
  • Language: English
  • DOI: 10.1007/s00216-023-04902-5
  • ISSN: 1618-2642; 1618-2650
  • Keywords: Biochemistry ; Analytical Chemistry
  • Origination:
  • Footnote:
  • Description: <jats:title>Abstract</jats:title><jats:p>Advanced glycation end products (AGEs) form extracellular crosslinking with collagenous proteins, which contributes to the development of diabetic complications. In this study, AGEs-related pentosidine (PENT) crosslinks-induced structural and biochemical changes are studied using multimodal multiphoton imaging, Raman spectroscopy and atomic force microscopy (AFM). Decellularized equine pericardium (EP) was glycated with four ribose concentrations ranging between 5 and 200 mM and monitored for up to 30 days. Two-photon excited fluorescence (TPEF) and second harmonic generation (SHG) microscopic imaging probed elastin and collagen fibers, respectively. The glycated EP showed a decrease in the SHG intensities associated with loss of non-centrosymmetry of collagen and an increase of TPEF intensities associated with PENT crosslinks upon glycation. TPEF signals from elastin fibers were unaffected. A three-dimensional reconstruction with SHG + TPEF z-stack images visualized the distribution of collagen and elastin within the EP volume matrix. In addition, Raman spectroscopy (RS) detected changes in collagen-related bands and discriminated glycated from untreated EP. Furthermore, AFM scans showed that the roughness increases and the D-unit structure of fibers remained unchanged during glycation. The PENT crosslinked-induced changes are discussed in the context of previous studies of glutaraldehyde- and genipin-induced crosslinking and collagenase-induced digestion of collagen. We conclude that TPEF, SHG, RS, and AFM are effective, label-free, and non-destructive methods to investigate glycated tissues, differentiate crosslinking processes, and characterize general collagen-associated and disease-related changes, in particular by their RS fingerprints.</jats:p>