Characterization of Riboflavin-modified Dentin Collagen Matrix
Characterization of Riboflavin-modified Dentin Collagen Matrix
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DOI：
10.1177/0022034512459053
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发表时间：
2012-11-01
影响因子：
7.6
通讯作者：
Neo, J.
中科院分区：
文献类型：
--
作者：
Fawzy, A.;Nitisusanta, L.;Neo, J.
交联被认为是增加牙本质胶原基质的机械和结构稳定性以及抗生物降解性的可能方法。本研究的目的是探讨机械和化学变化和胶原降解阻力与交联的牙本质胶原基质与UVA激活核黄素。牙本质胶原基质标本分别用0.1%和1%核黄素处理2 min，再用7 mW/cm 2 UVA（368 nm）光活化2 min，用原子力显微镜（AFM）和扫描电镜（SEM）观察胶原酶作用下牙本质胶原网络结构的变化。通过纳米压痕、常规力学测试和不同时间点的羟脯氨酸释放来表征表面/本体力学性能和生物降解抗性的变化。通过显微拉曼光谱分析与核黄素/胶原-基质相互作用相关的化学变化。UVA激活的核黄素增加了牙本质胶原基质的机械性能、机械稳定性和抗生物降解性。发现交联具有更高的胶原蛋白网络结构抵抗胶原蛋白溶解挑战的能力。显微拉曼光谱显示，某些拉曼谱带（1242-1667 cm（-1））在强度和波数上与交联有很强的依赖性，表明胶原蛋白/核黄素相互作用。与0.1%核黄素相比，UVA激活的核黄素（1%）在相对临床可接受的时间范围内更有效地交联牙本质胶原基质。
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.