Effect of corneal collagen crosslinking on viscoelastic shear properties of the cornea

Hatami-Marbini, Hamed; Emu, Md Esharuzzaman

doi:10.1016/j.jmbbm.2022.105300

Cited by 5 publications

(2 citation statements)

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“…Collagen, the most common structural protein in humans and other vertebrates, is an essential component of human cornea, tendon, skin, bone, and cartilage, providing mechanical stability, elasticity, and strength to organisms [1][2][3][4][5]. At present, 29 kinds of collagen are known, among which type I collagen is the most widely studied [6,7].…”

Section: Introductionmentioning

confidence: 99%

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Effect of Mechanical Microenvironment on Collagen Self-Assembly In Vitro

Han

Lin

et al. 2023

JFB

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Collagen, as a structural protein, is widely distributed in the human body. Many factors influence collagen self-assembly in vitro, including physical-chemical conditions and mechanical microenvironment, and play a key role in driving the structure and arrangement. However, the exact mechanism is unknown. The purpose of this paper is to investigate the changes in the structure and morphology of collagen self-assembly in vitro under mechanical microenvironment, as well as the critical role of hyaluronic acid in this process. Using bovine type I collagen as the research object, collagen solution is loaded into tensile and stress-strain gradient devices. The morphology and distribution of collagen is observed using an atomic force microscope while changing the concentration of collagen solution, mechanical loading strength, tensile speed, and ratio of collagen to hyaluronic acid. The results demonstrate that the mechanics field governs collagen fibers and changes their orientation. Stress magnifies the differences in results caused by different stress concentrations and sizes, and hyaluronic acid improves collagen fiber orientation. This research is critical for expanding the use of collagen-based biomaterials in tissue engineering.

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Section: Introductionmentioning

confidence: 99%

“…At present, 29 kinds of collagen are known, among which type I collagen is the most widely studied [6,7]. Collagen self-assembly is the complex layered process from molecular to macroscale length [1,2]. Each collagen molecule, which is made up of three mutually helical peptide chains, is about 300 nm in length and 1.5 nm in diameter.…”

Section: Introductionmentioning

confidence: 99%