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The corneal and scleral collagen matrix is the primary structural component of the eye's outer fibrous tunic, consisting mainly of Type I collagen fibrils interspersed with Type V and VI collagen and proteoglycans [1]. In the cornea, these fibrils are organized into highly ordered lamellae that provide the mechanical strength required to maintain curvature while ensuring optical transparency [2]. The scleral matrix, though less ordered, provides the structural integrity necessary to resist intraocular pressure and maintain the axial length of the eye [3]. Pathological degradation or biomechanical weakening of this matrix is central to the progression of keratoconus, corneal ectasia, and high myopia [4]. Therapeutic strategies targeting this matrix, such as corneal collagen cross-linking (CXL), involve the use of photosensitizers like riboflavin and ultraviolet-A (UV-A) light to create new covalent bonds between collagen molecules, thereby stiffening the tissue and halting disease progression [5]. Emerging research also explores scleral cross-linking as a method to prevent the axial elongation associated with progressive myopia by reinforcing the posterior ocular wall [6].
Induction of covalent cross-links between collagen fibrils via photo-oxidation (e.g., Riboflavin/UV-A) or chemical reaction to increase biomechanical stiffness and resistance to enzymatic degradation.
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