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Corneal stromal collagen fibrils are the fundamental structural units of the eye's stroma, comprising approximately 90% of the corneal thickness. These fibrils, primarily composed of Type I and Type V collagen, are organized into parallel arrays called lamellae, which are essential for maintaining the cornea's shape and refractive power (Meek & Knupp, 2015). The precise, uniform diameter and spacing of these fibrils are critical for optical transparency, as they minimize light scattering through destructive interference. In diseases like keratoconus, the organization of these fibrils is disrupted, leading to biomechanical weakening and progressive corneal thinning (NIH/NEI). Therapeutic intervention often targets these fibrils through corneal collagen cross-linking (CXL), where riboflavin and UVA light are used to induce covalent bonds between collagen molecules (Wollensak et al., 2003). This modification increases the mechanical stiffness of the stroma, effectively halting the progression of corneal ectasia and improving visual outcomes for patients.
Photo-oxidative cross-linking (generation of reactive oxygen species to induce covalent bond formation between collagen molecules) and chemical cross-linking to increase tissue stiffness.
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