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Proceedings Paper

Fluorescence spectroscopy of collagen crosslinking: non-invasive and in-situ evaluation of corneal stiffness
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Paper Abstract

Collagen is a long fibrous structural protein that imparts mechanical support, strength and elasticity to many tissues. The state of the tissue mechanical environment is related to tissue physiology, disease and function. In the cornea, the collagen network is responsible for its shape and clarity; disruption of this network results in degradation of visual acuity, for example in the keratoconus eye disease. The objective of the present study is to investigate the feasibility of using the endogenous fluorescence of collagen crosslinks to evaluate variations in the mechanical state of tissue, in particular, the stiffness of cornea in response to different degrees of photo-crosslinking or RGX treatment—a novel keratoconus treatment. After removing the epithelium, rabbit corneas were stained with Rose Bengal and then irradiated with a 532 nm solid-state laser. Analysis of the excitation spectra obtained by fluorescence spectroscopy shows a correlation between the fluorescence intensity at 370/460 nm excitation/emission wavelengths and the mechanical properties. In principle, it may be feasible to use the endogenous fluorescence of collagen crosslinks to evaluate the mechanical stiffness of cornea non-invasively and in situ.

Paper Details

Date Published: 6 March 2015
PDF: 6 pages
Proc. SPIE 9327, Optical Elastography and Tissue Biomechanics II, 93270R (6 March 2015); doi: 10.1117/12.2083702
Show Author Affiliations
Walfre Franco, Wellman Ctr. for Photomedicine (United States)
Antonio Ortega-Martinez, Wellman Ctr. for Photomedicine (United States)
Hong Zhu, Wellman Ctr. for Photomedicine (United States)
Ruisheng Wang, Clarkson Univ. (United States)
Irene E. Kochevar, Wellman Ctr. for Photomedicine (United States)


Published in SPIE Proceedings Vol. 9327:
Optical Elastography and Tissue Biomechanics II
Kirill V. Larin; David D. Sampson, Editor(s)

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