Collagen-collagen interactions mediated by plant-derived proanthocyanidins: A spectroscopic and atomic force microscopy study

Vidal C. M. P., Zhu W., Manohar S., Aydin B., Keiderling T. A., Messersmith P. B., ...More

ACTA BIOMATERIALIA, vol.41, pp.110-118, 2016 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 41
  • Publication Date: 2016
  • Doi Number: 10.1016/j.actbio.2016.05.026
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.110-118
  • Keywords: Collagen cross-linking, Dentin, Proanthocyanidins, Atomic force microscopy, ATR-FTIR spectroscopy, CROSS-LINKING, I COLLAGEN, DENTIN COLLAGEN, CARBODIIMIDE, PROTEIN, MATRIX, PRECIPITATION, COMPLEXATION, POLYPHENOLS, TISSUES
  • Dokuz Eylül University Affiliated: No


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.