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Current Directions in Biomedical Engineering

Joint Journal of the German Society for Biomedical Engineering in VDE and the Austrian and Swiss Societies for Biomedical Engineering

Editor-in-Chief: Dössel, Olaf

Editorial Board: Augat, Peter / Buzug, Thorsten M. / Haueisen, Jens / Jockenhoevel, Stefan / Knaup-Gregori, Petra / Kraft, Marc / Lenarz, Thomas / Leonhardt, Steffen / Malberg, Hagen / Penzel, Thomas / Plank, Gernot / Radermacher, Klaus M. / Schkommodau, Erik / Stieglitz, Thomas / Urban, Gerald A.

CiteScore 2018: 0.47

Source Normalized Impact per Paper (SNIP) 2018: 0.377

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Molecular processes of corneal collagen cross-linking in keratoconus therapy

Steven Melcher
  • Corresponding author
  • Technische Universität Dresden, Carl Gustav Carus Faculty of Medicine, Anesthesiology and Critical Care Medicine, Clinical Sensoring and Monitoring, Fetscherstraße, Dresden, Germany
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/ Eberhard Spörl / Edmund Koch / Gerald Steiner
Published Online: 2018-09-22 | DOI: https://doi.org/10.1515/cdbme-2018-0117


Corneal collagen cross-linking (CXL) with riboflavin and UVA light is a therapeutic procedure to restore the mechanical stability of corneal tissue. The treatment method applies to pathological tissue changes, such as keratoconus. It induces the photochemical formation of new collagen cross-links. Although therapeutic effects are indisputable, the exact molecular process of CXL and how cross-links are formed is still unclear. In this work, Fouriertransform infrared (FT-IR) spectroscopy is used to investigate the cross-linking process. For that purpose, in-situ experiments with porcine corneas are carried out using attenuated total reflection (ATR) spectroscopy. Furthermore, IR micro-spectroscopic imaging in transmission mode is used to investigate thin tissue sections of the cornea and initial approaches for the distinction of cross-linked and untreated tissue by IR microspectroscopic imaging were performed. Multivariate methods are applied to access changes that occur as a result of CXL. It is shown that spectral changes after cross-linking are caused predominantly by an increase of methyl- and methylene groups as well as primary and secondary amines. In addition, a decrease of carbonyl groups could be observed.

Keywords: Corneal collagen crosslinking; FT-IR spectroscopy; microspectroscopic imaging; attenuated total reflection

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Published Online: 2018-09-22

Published in Print: 2018-09-01

Citation Information: Current Directions in Biomedical Engineering, Volume 4, Issue 1, Pages 489–492, ISSN (Online) 2364-5504, DOI: https://doi.org/10.1515/cdbme-2018-0117.

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