Effect of cross-linking with riboflavin and ultraviolet A on the chemical bonds and ultrastructure of human sclera

Jung, Gyeong-Bok; Lee, Hui-Jae; Kim, Jihye; Lim, Jong In; Choi, Samjin; Jin, Kyung Hyun; Park, Hun-Kuk

doi:10.1117/1.3662458

Cited by 26 publications

(32 citation statements)

References 34 publications

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“…Micro-Raman analysis revealed characteristic accentuation and shift in both amide-I and -III bands with crosslinking, which is consistent with previous reports of collagen type-I crosslinked with riboflavin (Jung et al, 2011) or glutaraldehyde (Jastrzebska et al, 2003). In addition, the amide-I band was associated with the stretching-vibration of the peptide carbonyl groups, whereas the amide-III band resulted from the NH in-plane deformation coupled to CN-stretching.…”

Section: Discussionsupporting

confidence: 88%

Characterization of Riboflavin-modified Dentin Collagen Matrix

et al. 2012

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Crosslinking is considered a possible approach to increasing the mechanical and structural stability and biodegradation resistance of the dentin collagen matrix. The aim of this study was to investigate the mechanical and chemical variations and collagen degradation resistance associated with crosslinking of the dentin collagen matrix with UVA-activated riboflavin. Dentin collagen matrix specimens were treated with 0.1 and 1% riboflavin for 2 min and photo-activated with 7 mW/cm(2) UVA (368 nm) for 2 min. The structural change of the dentin collagen network with collagenase exposure was investigated by AFM and SEM at different time-points. The variations in surface/bulk mechanical properties and biodegradation resistance were characterized by nano-indentation, conventional mechanical testing, and hydroxyproline liberation at different time-points. Chemical changes associated with riboflavin/collagen-matrix interaction were analyzed by micro-Raman spectroscopy. UVA-activated riboflavin increased the mechanical properties, mechanical stability, and biodegradation resistance of the dentin collagen matrix. Higher collagen-network structural resistance against collagenolytic challenges was found with crosslinking. micro-Raman spectroscopy showed a strong dependency, in both intensity and wave-number, of certain Raman bands (1242-1667 cm(-1)) with crosslinking indicating the collagen/riboflavin interactions. UVA-activated riboflavin (1%) more efficiently crosslinked the dentin collagen matrix within a relatively clinically acceptable time-frame compared with 0.1% riboflavin.

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Section: Discussionsupporting

confidence: 88%

Characterization of Riboflavin-modified Dentin Collagen Matrix

et al. 2012

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“…The UV dose‐dependent stiffness controllability was further demonstrated by the FTIR spectroscopic analysis given that the chemical changes in the compressed collagen construct can alter the IR absorption in the FTIR spectroscopic analysis. Previous studies showed that an increase in peak values of the amide bands is associated with the riboflavin‐mediated crosslinking and consequent stiffness increase (Chan, Choy, & Lai, ; Jung et al, ). The gradual changes of the IR absorptions, at amide A, I, II, and III bands, in this study indicated the UV dose‐dependent covalent bonds formation, which was similar to the trend observed in previous studies.…”

Section: Discussionmentioning

confidence: 99%

Grayscale mask‐assisted photochemical crosslinking for a dense collagen construct with stiffness gradient

et al. 2019

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Despite the potential of a collagen construct with a stiffness gradient for investigating cell–extracellular matrix (ECM) stiffness interaction or recapitulating an in vivo tissue interface, it has been developed in a limited way due to the low and poorly controllable mechanical properties of the collagen. This study proposes a novel fabrication process to achieve a compressed collagen construct with a stiffness gradient, named COSDIENT, at a level of ~ 1 MPa while maintaining in vivo ECM‐like dense collagen fibrillar structures. The COSDIENT was fabricated by collagen compression followed by grayscale mask‐assisted UV–riboflavin crosslinking. The collagen compression process enabled the remarkable increase in the stiffness of the collagen gel from ~ 1–10 kPa to ~ 1 MPa by physical compaction. The subsequent UV–riboflavin crosslinking with a continuous‐tone grayscale mask could simply generate a gradual change of UV irradiation followed by modulating riboflavin‐mediated crosslinking, thereby resulting in a continuous stiffness gradient with a range of 1.16–4.38 MPa in the single compressed collagen construct. The suggested grayscale mask‐assisted photochemical crosslinking had no effect on the physical and optical properties of the original compressed collagen construct, while inducing gradual changes of chemical bonds among collagen fibrils. A skin wound healing assay with epidermal keratinocytes was finally applied as an application example of the COSDIENT to examine the effect of stiffness on the skin keratinocyte behavior.

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“…More recently, physical methods, specifically ultraviolet radiation, have been tried in dentistry and in ophthalmology . Ultraviolet (UVA)‐activated riboflavin has been shown to increase bond strength, stabilize the adhesive interface, and inhibit dentin MMPs .…”

Section: Methods To Increase the Durability Of Dentin Bondsmentioning

confidence: 99%

Dentin Adhesion and MMPs: A Comprehensive Review

Perdigão

Reis

Loguércio

2013

J Esthet Restor Dent

178

169

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This review examines the fundamental processes responsible for the aging mechanisms involved in the degradation of resin-bonded interfaces, as well as some potential approaches to prevent and counteract this degradation. Current research in several research centers aims at increasing the resin-dentin bond durability. The hydrophilic and acidic characteristics of current dentin adhesives have made hybrid layers highly prone to water sorption. This, in turn, causes polymer degradation and results in decreased resin-dentin bond strength over time. These unstable polymers inside the hybrid layer may result in denuded collagen fibers, which become vulnerable to mechanical and hydrolytical fatigue, as well as degradation by host-derived proteases with collagenolytic activity. These enzymes, such as matrix metalloproteinases and cysteine cathepsins, have a crucial role in the degradation of type I collagen, the organic component of the hybrid layer. This review will also describe several methods that have been recently advocated to silent the activity of these endogenous proteases.

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Effect of cross-linking with riboflavin and ultraviolet A on the chemical bonds and ultrastructure of human sclera

Cited by 26 publications

References 34 publications

Characterization of Riboflavin-modified Dentin Collagen Matrix

Characterization of Riboflavin-modified Dentin Collagen Matrix

Grayscale mask‐assisted photochemical crosslinking for a dense collagen construct with stiffness gradient

Dentin Adhesion and MMPs: A Comprehensive Review

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