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天然交联剂稳定胶原蛋白:超薄片层牙本质胶原模型的定性和定量傅里叶变换红外光谱研究。

Collagen stabilization by natural cross-linkers: A qualitative and quantitative FTIR study on ultra-thin dentin collagen model.

机构信息

Department of Oral and Craniofacial Sciences, School of Dentistry, University of Missouri-Kansas City.

出版信息

Dent Mater J. 2022 May 31;41(3):440-450. doi: 10.4012/dmj.2021-247. Epub 2022 Mar 4.

DOI:10.4012/dmj.2021-247
PMID:35249902
Abstract

Due to its low tolerance to external factors such as enzymes, dentin collagen often requires stabilization, which can be achieved through cross-linking. In this study, qualitative and quantitative Fourier transform infrared (FTIR) analyses were used to assess dentin collagen stabilization effects of three structurally-different flavonoids -A-type linkage proanthocyanidins (A-PA), B-type linkage proanthocyanidins (B-PA), and epigallocatechin gallate (EGCG), all from natural extracts. Particularly, transmission FTIR spectroscopy was used for the first time to quantitatively assess the biodegradation of fresh ultra-thin (10 µm) dentin collagen films caused by collagenase digestion. Two traditional analytical methods, namely the hydroxyproline assay and weight loss analysis, were also used for comparison purposes. The results from all three methods showed consistently that A-PA and B-PA provide better collagen stabilization than EGCG at concentrations of 0.65% and 1.3% (p<0.01). FTIR is demonstrated to be a valuable and reliable analytical tool for qualitative and quantitative evaluation of ultra-thin collagen films.

摘要

由于其对外界因素(如酶)的低耐受性,牙本质胶原通常需要稳定化,这可以通过交联来实现。在这项研究中,使用定性和定量傅里叶变换红外(FTIR)分析来评估三种结构不同的类黄酮——A型连接原花青素(A-PA)、B 型连接原花青素(B-PA)和表没食子儿茶素没食子酸酯(EGCG)对牙本质胶原的稳定化效果,它们均来自天然提取物。特别是,首次使用传输 FTIR 光谱法定量评估了胶原酶消化引起的新鲜超薄(10 µm)牙本质胶原膜的生物降解。两种传统的分析方法,即羟脯氨酸测定法和失重分析也被用于比较。这三种方法的结果都一致表明,A-PA 和 B-PA 在 0.65%和 1.3%的浓度下比 EGCG 提供更好的胶原稳定性(p<0.01)。FTIR 被证明是一种有价值且可靠的分析工具,可用于定性和定量评估超薄胶原膜。

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