In the cornea of the eye light transmission is facilitated by the regular arrangement and uniform diameter of collagen fibrils that constitute the bulk of the extracellular corneal matrix. Matrix architecture, in turn, is believed to be governed by interactions between collagen fibrils and proteoglycan molecules modified with sulfated glycosaminoglycan side chains. Here, we outline the contribution made by small-angle X-ray scattering studies of the cornea in understanding the role of sulfated glycosaminoglycans in the control of collagen architecture in cornea, and present new depth-profiled microbeam data from swollen human eye-bank corneas that indicate no significant change in collagen fibril diameter throughout the tissue, but a lower collagen interfibrillar spacing in the anterior-most stromal regions compared with the ultrastructure of the deeper cornea. © International Union of Crystallography 2007.
CITATION STYLE
Quantock, A. J., Boote, C., Young, R. D., Hayes, S., Tanioka, H., Kawasaki, S., … Meek, K. M. (2007). Small-angle fibre diffraction studies of corneal matrix structure: A depth-profiled investigation of the human eye-bank cornea. In Journal of Applied Crystallography (Vol. 40). https://doi.org/10.1107/S0021889807005523
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