Collagen-collagen interactions mediated by plant-derived proanthocyanidins: A spectroscopic and atomic force microscopy study.
Collagen-collagen interactions mediated by plant-derived proanthocyanidins: A spectroscopic and atomic force microscopy study.
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DOI：
10.1016/j.actbio.2016.05.026
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发表时间：
2016-09-01
影响因子：
9.7
通讯作者：
Bedran-Russo AK
中科院分区：
文献类型：
--
作者：
Vidal CM;Zhu W;Manohar S;Aydin B;Keiderling TA;Messersmith PB;Bedran-Russo AK
胶原交联是生物组织稳定性和功能的决定因素。植物源性原花青素（PAC）通过非酶相互作用模拟不同层次的胶原交联，从而增强富含胶原的组织（如牙本质）的生物力学和生物稳定性。本研究通过荧光光谱分析研究了来自葡萄属葡萄籽提取物的PAC与溶解形式和脱矿牙本质基质（DDM）中的I型胶原的相互作用;通过原子力显微镜（AFM）研究了交联溶液存在下胶原-胶原结合力;并使用衰减全反射傅立叶变换红外光谱（ATR-FTIR）对DDM进行了光谱分析。选择具有已知交联机制的戊二醛（GA）和碳化二亚胺盐酸盐（EDC）进行比较分析。溶解的I型胶原蛋白与PAC、EDC和GA相互作用后荧光的变化反映了胶原蛋白构象的明显改变。PAC也比EDC和GA促进更强的胶原-胶原纤维相互作用。使用ATR-FTIR光谱分析在PAC处理的胶原和DDM中观察到一个新的特征。研究结果表明胶原蛋白和PAC之间存在共价相互作用。PAC-胶原之间的相互作用机制具有吸引力和有前途的组织定制的生物医学应用和潜在驱动这种相互作用的结合力的特征。
Collagen cross-linkings are determinant of biological tissue stability and function. Plant-derived proanthocyanidins (PACs) mimic different hierarchical levels of collagen cross-links by non-enzymatic interactions resulting in the enhancement to the biomechanics and biostability of collagen-rich tissues such as dentin. This study investigated the interaction of PACs from Vitis vinifera grape seed extract with type I collagen in solubilized form and in the demineralized dentin matrix (DDM) by fluorescence spectral analysis; collagen-collagen binding forces in presence of cross-linking solutions by atomic force microscopy (AFM); and spectroscopic analysis of the DDM using attenuated total reflectance Fourier transform-infrared spectroscopy (ATR-FTIR). Glutaraldehyde (GA) and carbodiimide hydrochloride (EDC) with known cross-linking mechanisms were selected for comparative analyses. Changes in fluorescence upon interaction of solubilized type I collagen with PACs, EDC and GA reflected pronounced modifications in collagen conformation. PACs also promoted stronger collagen-collagen fibrils interaction than EDC and GA. A new feature was observed using ATR-FTIR spectroscopic analysis in PACs-treated collagen and DDM. The findings suggest covalent interactions between collagen and PACs. The mechanisms of interaction between PACs-collagen hold attractive and promising tissue-tailored biomedical applications and the binding forces that potentially drive such interaction were characterized.