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

Cristina M.P Vidal; Weiying Zhu; Suresh Manohar; Berdan Aydin; Timothy A Keiderling; Phillip B Messersmith; Ana K Bedran-Russo

doi:10.1016/j.actbio.2016.05.026

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

Journal article

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

Cristina M.P Vidal, Weiying Zhu, Suresh Manohar, Berdan Aydin, Timothy A Keiderling, Phillip B Messersmith and Ana K Bedran-Russo

Acta biomaterialia, Vol.41, pp.110-118

09/01/2016

DOI: 10.1016/j.actbio.2016.05.026

PMCID: PMC4983101

PMID: 27208639

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Abstract

[Display omitted] 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. Connective tissues such as skin, bone and dentin are mainly composed of type I collagen, which is cross-linked to promote tissue stability, strength and function. Novel therapies using substances that mimic cross-links have been proposed to promote repair of collagen-based-tissues. In dentistry, naturally occurring proanthocyanidins (PACs) have the potential to enhance dentin mechanical properties and reduce its enzymatic degradation, but their mechanisms of cross-linking are unclear. The present study investigated the specific interactions between PACs-type I collagen in purified and dentin collagen and compared to the well described cross-linking mechanisms promoted by synthetic chemical substances. Findings reveal that covalent-like bonds are induced by plant PACs in type I collagen as well as in complex dental native tissue, promoting strong collagen-collagen interactions.

Atomic Force Microscopy

Dentin

ATR-FTIR spectroscopy

Collagen cross-linking

Proanthocyanidins

Details

Title: Subtitle: Collagen-collagen interactions mediated by plant-derived proanthocyanidins: A spectroscopic and atomic force microscopy study
Creators: Cristina M.P Vidal - College of Dentistry, University of Illinois at Chicago, 801 South Paulina Street, Chicago, IL 60612, USA
Weiying Zhu - Department of Chemistry, University of Illinois at Chicago, 845 West Taylor Street, Chicago, IL 60607, USA
Suresh Manohar - Biomedical Engineering Department, McCormick School of Engineering, Northwestern University, Technological Institute, 2145 Sheridan Road, Evanston, IL 60208, USA
Berdan Aydin - College of Dentistry, University of Illinois at Chicago, 801 South Paulina Street, Chicago, IL 60612, USA
Timothy A Keiderling - Department of Chemistry, University of Illinois at Chicago, 845 West Taylor Street, Chicago, IL 60607, USA
Phillip B Messersmith - Biomedical Engineering Department, McCormick School of Engineering, Northwestern University, Technological Institute, 2145 Sheridan Road, Evanston, IL 60208, USA
Ana K Bedran-Russo - College of Dentistry, University of Illinois at Chicago, 801 South Paulina Street, Chicago, IL 60612, USA
Resource Type: Journal article
Publication Details: Acta biomaterialia, Vol.41, pp.110-118
DOI: 10.1016/j.actbio.2016.05.026
PMID: 27208639
PMCID: PMC4983101
NLM abbreviation: Acta Biomater
ISSN: 1742-7061
eISSN: 1878-7568
Publisher: Elsevier Ltd
Grant note: DOI: 10.13039/100000002, name: NIH; DOI: 10.13039/100000072, name: NIDCR
Language: English
Date published: 09/01/2016
Academic Unit: Operative Dentistry
Record Identifier: 9984065701302771

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