Dentin collagen denaturation status assessed by collagen hybridizing peptide and its effect on bio-stabilization of proanthocyanidins.
Dentin collagen denaturation status assessed by collagen hybridizing peptide and its effect on bio-stabilization of proanthocyanidins.
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DOI：
10.1016/j.dental.2022.04.020
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发表时间：
2022-05
期刊：
影响因子：
5
通讯作者：
Wang, Yong
中科院分区：
文献类型：
--
作者：
Wang, Rong;Nisar, Saleha;Vogel, Zachary;Liu, Hang;Wang, Yong
关键词：
目的探讨胶原杂交肽（CHP）和磷酸处理对牙本质胶原变性的影响，并探讨胶原变性对原花青素（PA）促进牙本质生物稳定性的影响。将人磨牙切成7 μm厚的牙本质膜，进行脱矿处理，分为PA修饰组、h3po4处理的胶原蛋白修饰组、酶处理的胶原蛋白修饰组和未修饰组。PA修饰包括将胶原膜浸泡在0.65% PA中30秒。采用H3PO4和酶处理实验性诱导胶原变性，通过荧光共轭chp （F-CHP）染色的荧光强度（FI）进行定量（n=4）。FTIR用于表征胶原结构。采用减重法和羟脯氨酸法（n=6），对各组进行胶原酶消化，检测PA对变性胶原的生物稳定作用。采用双因素方差分析和game - howell事后检验对数据进行分析（α=0.05）。FTIR显示变性处理后胶原的二次结构变化，证实了PA在对照和处理胶原中的掺入和交联。F-CHP染色表明h3po4处理（FI=83.22）、酶处理（FI=36.54）和对照组（FI=6.01）的胶原变性程度分别为高、中、低。PA修饰显著降低了各组的减重和羟脯氨酸消化释放量（p<0.0001），其结果与FI值的相关性为r= 0.96-0.98。本文首次介绍了一种用于牙本质胶原变性定量检测的分子法CHP。PA改性能有效地稳定变性胶原蛋白，使其抗胶原酶消化，稳定效果与胶原蛋白变性程度呈负相关。
To assess dentin collagen denaturation from phosphoric acid and enzyme treatments using collagen hybridizing peptide (CHP) and to investigate the effect of collagen denaturation on bio-stabilization promoted by proanthocyanidins (PA). Human molars were sectioned into 7-μm-thick dentin films, demineralized, and assigned to six groups: control with/without PA modification, H3PO4-treated collagen with/without PA modification, enzyme-treated collagen with/without PA modification. PA modification involved immersing collagen films in 0.65% PA for 30 seconds. H3PO4 and enzyme treatments were used to experimentally induce collagen denaturation, which was quantitated by fluorescence intensity (FI) from the fluorescently-conjugated-CHP (F-CHP) staining (n=4). FTIR was used to characterize collagen structures. All groups were subject to collagenase digestion to test the bio-stabilization effect of PA on denatured collagen using weight loss analysis and hydroxyproline assay (n=6). Data were analyzed using two-factor ANOVA and Games-Howell post hoc tests (α=0.05). FTIR showed collagen secondary structural changes after denaturation treatments and confirmed the incorporation and cross-linking of PA in control and treated collagen. F-CHP staining indicated high-degree, medium-degree, and low-degree collagen denaturation from H3PO4-treatment (FI=83.22), enzyme-treatment (FI=36.54), and control (FI=6.01) respectively. PA modification significantly reduced the weight loss and hydroxyproline release of all groups from digestion (p<0.0001), with the results correlated with FI values at r=0.96–0.98. A molecular method CHP is introduced as a sensitive technique to quantitate dentin collagen denaturation for the first time. PA modification is shown to effectively stabilize denatured collagen against collagenase digestion, with the stabilization effect negatively associated with the collagen denaturation degree.
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DOI：
10.1016/j.jmbbm.2011.05.003
发表时间：
2011-10
影响因子：
3.9
作者：
Castellan, Carina Strano;Bedran-Russo, Ana Karina;Karol, Sachin;Rodrigues Pereira, Patricia Nobrega
通讯作者：
Rodrigues Pereira, Patricia Nobrega
影响因子：
5
作者：
Eliades, G;Vougiouklakis, G;Palaghias, G
通讯作者：
Palaghias, G
DOI：
10.1002/jbm.b.31295
发表时间：
2009-07
影响因子：
3.4
作者：
Carrilho, Marcela R.;Tay, Franklin R.;Donnelly, Adam M.;Agee, Kelli A.;Tjaederhane, Leo;Mazzoni, Annalisa;Breschi, Lorenzo;Foulger, Stephen;Pashley, David H.
通讯作者：
Pashley, David H.
影响因子：
4.4
作者：
Green B;Yao X;Ganguly A;Xu C;Dusevich V;Walker MP;Wang Y
通讯作者：
Wang Y
影响因子：
5
作者：
Breschi, Lorenzo;Maravic, Tatjana;Mazzoni, Annalisa
通讯作者：
Mazzoni, Annalisa