Characterization of genipin-modified dentin collagen.
Characterization of genipin-modified dentin collagen.
复制标题
京尼平修饰的牙本质胶原蛋白的表征。
DOI：
10.1155/2014/702821
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发表时间：
2014
影响因子：
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通讯作者：
Yamauchi,Mitsuo
中科院分区：
文献类型：
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作者：
Nagaoka,Hiroko;Nagaoka,Hideaki;Walter,Ricardo;Boushell,LeeW;Miguez,PatriciaA;Burton,Andrew;Ritter,AndréV;Yamauchi,Mitsuo
牙本质生物改性技术的应用可以改善牙本质的生物化学和生物力学性能。几种胶原交联剂已被报道可以增强牙本质的力学性能。然而，经过剂诱导生物修饰的胶原蛋白的特性尚不清楚。本研究的目的是分析天然交联剂genipin （GE）对牙本质变色、胶原稳定性、氨基酸组成和赖氨酸氧化酶介导的天然胶原交联的变化的影响。用三种不同浓度的GE（0.01%、0.1%和0.5%）处理牛牙本质胶原，处理数次（0-24 h）。通过氨基酸和交联分析表征了NaB3H4还原胶原的生化特性变化。用GE处理牙本质胶原导致了浓度和时间依赖性的色素沉着和抗细菌胶原酶的稳定性。赖氨酸氧化酶介导的三价成熟交联吡啶啉在各组之间没有差异，而在0.5% GE处理24 h的胶原中，主要的二价未成熟交联脱氢二羟赖氨酸氨基亮氨酸/其酮胺显著低于对照组（P<0.05）。新形成的GE诱导的交联很可能以浓度依赖的方式涉及胶原蛋白的赖氨酸和羟赖氨酸残基。其中一些交联似乎可以被NaB3H4还原和稳定。
Application of biomodification techniques to dentin can improve its biochemical and biomechanical properties. Several collagen cross‐linking agents have been reported to strengthen the mechanical properties of dentin. However, the characteristics of collagen that has undergone agent‐induced biomodification are not well understood. The objective of this study was to analyze the effects of a natural cross‐linking agent, genipin (GE), on dentin discoloration, collagen stability, and changes in amino acid composition and lysyl oxidase mediated natural collagen cross‐links. Dentin collagen obtained from extracted bovine teeth was treated with three different concentrations of GE (0.01%, 0.1%, and 0.5%) for several treatment times (0–24 h). Changes in biochemical properties of NaB3H4‐reduced collagen were characterized by amino acid and cross‐link analyses. The treatment of dentin collagen with GE resulted in a concentration‐ and time‐dependent pigmentation and stability against bacterial collagenase. The lysyl oxidase‐mediated trivalent mature cross‐link, pyridinoline, showed no difference among all groups while the major divalent immature cross‐link, dehydro‐dihydroxylysinonorleucine/its ketoamine in collagen treated with 0.5% GE for 24 h, significantly decreased compared to control (P<0.05). The newly formed GE‐induced cross‐links most likely involve lysine and hydroxylysine residues of collagen in a concentration‐dependent manner. Some of these cross‐links appear to be reducible and stabilized with NaB3H4.