Binding affinity of proanthocyanidin from waste Pinus radiata bark onto proline-rich bovine achilles tendon collagen type I

Ku, Chang Sub; Sathishkumar, M.; Mun, Sung Phil

doi:10.1016/j.chemosphere.2006.11.037

Cited by 90 publications

(70 citation statements)

References 36 publications

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“…The use of 20% TA at pH 7.4 followed previous studies (Bedran-Russo et al, 2007) in which cross-linking solutions had their pH adjusted to a neutral level. Such a pH is more desirable, since it would have low impact on the undemineralized dentin and also on the mechanism of TA-collagen interaction (Ku et al, 2007). It has been reported that the interaction of proanthocyanidin (also a condensed tannin) with proline-rich proteins is pH-dependent, in which the greatest precipitation was found to be near the isoelectric point of protein (Bennick, 2002).…”

Section: Discussionmentioning

confidence: 99%

Mechanical Properties of Tannic-acid-treated Dentin Matrix

et al. 2009

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Dentin collagen is a major component of the hybrid layer, and its stability may have a great impact on the properties of adhesive interfaces. We tested the hypothesis that the use of tannic acid (TA), a collagen cross-linking agent, may affect the mechanical properties and stability of the dentin matrix. The present study evaluated the effects of different concentrations of TA on the modulus of elasticity and enzymatic degradation of dentin matrix. Hence, the effect of TA pre-treatment on resin-dentin bond strength was assessed with the use of two bonding systems. Sound human molars were used and prepared according to each experimental design. The use of TA affected the properties of demineralized dentin by increasing its stiffness. TA treatment inhi bited the effect of collagenase digestion on dentin matrix, particularly for 10%TA and 20%TA. The TA-dentin matrix complex resulted in improved bond strength for both adhesive systems.

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Section: Discussionmentioning

confidence: 99%

Mechanical Properties of Tannic-acid-treated Dentin Matrix

et al. 2009

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“…The use of a proanthocyanidin-based cross-linking agent on demineralized dentin has been associated with a significant improvement in the mechanical and physical properties of dentin (Bedran-Russo et al, 2007. The 4 proposed mechanisms for interaction between proanthocyanidin and proteins include covalent (Pierpoint, 1969), ionic (Loomis, 1974), hydrogen bonding (Ku et al, 2007), and hydrophobic interactions (Han et al, 2003). Based on amino acid analysis, it is likely that grape seed extract induces cross-links via a mechanism different from that of glutaraldehyde, in which Lys and Hyl are involved (Ritter et al, 2001).…”

Section: Discussionmentioning

confidence: 99%

Effects of Chemical Cross-linkers on Caries-affected Dentin Bonding

2009

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A supplemental appendix to this article is published electronically only at http://jdr.sagepub.com/supplemental. AbstrAct The achievement of a strong and stable bond between composite resin and dentin remains a challenge in restorative dentistry. Over the past two decades, dental materials have been substantially improved, with better handling and bonding characteristics. However, little attention has been paid to the contribution of collagen structure/stability to bond strength. We hypothesized that the induction of cross-linking in dentin collagen improves dentin collagen stability and bond strength. This study investigated the effects of glutaraldehyde-and grape seed extract-induced cross-linking on the dentin bond strengths of sound and caries-affected dentin, and on the stability of dentin collagen. Our results demonstrated that the application of chemical cross-linking agents to etched dentin prior to bonding procedures significantly enhanced the dentin bond strengths of caries-affected and sound dentin. Glutaraldehyde and grape seed extract significantly increased dentin collagen stability in sound and caries-affected dentin, likely via distinct mechanisms.

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“…18 Proanthocyanidin is a natural collagen crosslinker 18 well known to readily precipitate proline-rich proteins (such as collagen) due to hydrogen and covalent bonds. 20 The Proanthocyanidin have been demonstrated to increase the ultimate tensile strength and elastic modulus of demineralized dentin. 14,40 According to the results obtained in this study, it could be concluded that type I collagen fibers from human dentin or bovine Achilles deep tendon are structurally similar when evaluated by ATR-FTIR spectroscopy.…”

Section: Discussionmentioning

confidence: 99%

“…9 For this in vitro analysis, ideally, the use of human dentin would be necessary. However, the difficulties inherent to this substrate, such as differences in mineralization, dentinal tubule dimensions, and the difficulty of obtaining teeth, make it necessary to use substitutes during chemical analyses, which suggests the use of type I collagen membranes, 20 and which has not yet been reported in the literature.…”

Section: Introductionmentioning

confidence: 99%

Effect of dental tissue conditioners and matrix metalloproteinase inhibitors on type I collagen microstructure analyzed by Fourier transform infrared spectroscopy

et al. 2012

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2012Effect of dental tissue conditioners and matrix metalloproteinase inhibitors on type I collagen microstructure analyzed by Fourier transform infrared spectroscopy JOURNAL OF BIOMEDICAL MATERIALS RESEARCH PART B-APPLIED BIOMATERIALS, MALDEN, v. 100B, n. 4, pp. 1009-1016, MAY, 2012 Abstract: This study aimed to evaluate the chemical interaction of collagen with some substances usually applied in dental treatments to increase the durability of adhesive restorations to dentin. Initially, the similarity between human dentin collagen and type I collagen obtained from commercial bovine membranes of Achilles deep tendon was compared by the Attenuated Total Reflectance technique of Fourier Transform Infrared (ATR-FTIR) spectroscopy. Finally, the effects of application of 35% phosphoric acid, 0.1M ethylenediaminetetraacetic acid (EDTA), 2% chlorhexidine, and 6.5% proanthocyanidin solution on microstructure of collagen and in the integrity of its triple helix were also evaluated by ATR-FTIR. It was observed that the commercial type I collagen can be used as an efficient substitute for demineralized human dentin in studies that use spectroscopy analysis. The 35% phosphoric acid significantly altered the organic content of amides, proline and hydroxyproline of type I collagen. The surface treatment with 0.1M EDTA, 2% chlorhexidine, or 6.5% proanthocyanidin did not promote deleterious structural changes to the collagen triple helix. The application of 6.5% proanthocyanidin on collagen promoted hydrogen bond formation.

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Binding affinity of proanthocyanidin from waste Pinus radiata bark onto proline-rich bovine achilles tendon collagen type I

Cited by 90 publications

References 36 publications

Mechanical Properties of Tannic-acid-treated Dentin Matrix

Mechanical Properties of Tannic-acid-treated Dentin Matrix

Effects of Chemical Cross-linkers on Caries-affected Dentin Bonding

Effect of dental tissue conditioners and matrix metalloproteinase inhibitors on type I collagen microstructure analyzed by Fourier transform infrared spectroscopy

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