Tannin interactions with a full‐length human salivary proline‐rich protein display a stronger affinity than with single proline‐rich repeats

Charlton, Adrian J.; Baxter, Nicola J.; Lilley, Terence H.; Haslam, Edwin; McDonald, Charles J.; Williamson, Michael P.

doi:10.1016/0014-5793(96)00186-x

Cited by 141 publications

(101 citation statements)

References 15 publications

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“…IB5, a 70-residue human BPRP, was selected for evaluation of the interaction of a naturally occurring PRP with polyphenols (Charlton et al ., 1996). This protein contains three 21-residue tandemly repeated regions, in contrast to the previously used peptide, which contained only one repeat region.…”

Section: (Viii) Interaction Of Salivary Proteins and Tanninmentioning

confidence: 99%

Interaction of Plant Polyphenols with Salivary Proteins

Bennick

2002

Critical Reviews in Oral Biology & Medicine

385

265

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Tannins are polyphenols that occur widespread in plant-based food. They are considered to be part of the plant defense system against environmental stressors. Tannins have a number of effects on animals, including growth-rate depression and inhibition of digestive enzymes. Tannins also have an effect on humans: They are, for example, the cause of byssinosis, a condition that is due to exposure to airborne tannin. Their biological effect is related to the great efficiency by which tannins precipitate proteins, an interaction that occurs by hydrophobic forces and hydrogen bonding. Two groups of salivary proteins, proline-rich proteins and histatins, are highly effective precipitators of tannin, and there is evidence that at least proline-rich proteins act as a first line of defense against tannins, perhaps by precipitating tannins in food and preventing their absorption from the alimentary canal. Proline plays an important role in the interaction of proline-rich proteins with tannins. In contrast, it is primarily basic residues that are responsible for the binding of histatins to tannin. The high concentration of tannin-binding proteins in human saliva may be related to the fruit and vegetable diet of human ancestors.

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Section: (Viii) Interaction Of Salivary Proteins and Tanninmentioning

confidence: 99%

Interaction of Plant Polyphenols with Salivary Proteins

Bennick

2002

Critical Reviews in Oral Biology & Medicine

385

265

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“…3 A number of studies have been reported on the binding properties of polyphenols to milk and salivary proteins, using various experimental techniques. [4][5][6][7] Studies on the binding properties of human biosubstsrate proteins are still limited.…”

Section: Introductionmentioning

confidence: 99%

Molecular and thermodynamic basis for EGCG‐Keratin interaction‐part I: Molecular dynamics simulations

et al. 2013

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Nonspecific binding of small molecules to proteins influences transdermal permeation and intestinal absorption, yet understanding of the molecular and thermodynamic basis is still limited. In this study, we report all-atom, fully solvated molecular dynamics simulations of the thermodynamic characteristics of epigallocatechin-3-gallate (EGCG) binding keratin. Experimental validation is reported in Part II. Herein, 18 μs of simulation sampling was calculated. We show that the binding process is a combination of hydrophobic interaction, hydrogen bonding and aromatic interaction. The umbrella sampling technique was used to calculate the binding free energy of EGCG with keratin segments. By extracting EGCG from the keratin-EGCG complex using steered molecular dynamics, the rupture force was observed to be linearly related to the binding free energy. Multilayer binding of EGCG clusters to keratin has been shown. The binding free energy of -6.2 kcal mol obtained from the simulations was in excellent agreement with the experimental Part II. © 2013 American Institute of Chemical Engineers

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“…Polyphenols have a hydrophobic internal core and numerous external hydroxyl groups. By virtue of this structure, they react with proteins, specifically binding to hydrophobic regions 37 but also establishing numerous hydrogen bonds, showing particularly high affinity for prolinerich proteins 38 such as collagen and elastin. 39 In addition, they are efficient antibacterial agents and reduce inflammation and antigenicity.…”

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confidence: 99%

Stabilized Collagen Scaffolds for Heart Valve Tissue Engineering

Tedder

Liao

Weed

et al. 2009

Tissue Engineering Part A

124

111

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Scaffolds for heart valve tissue engineering must function immediately after implantation but also need to tolerate cell infiltration and gradual remodeling. We hypothesized that moderately cross-linked collagen scaffolds would fulfill these requirements. To test our hypothesis, scaffolds prepared from decellularized porcine pericardium were treated with penta-galloyl glucose (PGG), a collagen-binding polyphenol, and tested for biodegradation, biaxial mechanical properties, and in vivo biocompatibility. For controls, we used un-cross-linked scaffolds and glutaraldehyde-treated scaffolds. Results confirmed complete pericardium decellularization and the ability of scaffolds to encourage fibroblast chemotaxis and to aid in creation of anatomically correct valve-shaped constructs. Glutaraldehyde cross-linking fully stabilized collagen but did not allow for tissue remodeling and calcified when implanted subdermally in rats. PGG-treated collagen was initially resistant to collagenase and then degraded gradually, indicating partial stabilization. Moreover, PGG-treated pericardium exhibited excellent biaxial mechanical properties, did not calcify in vivo, and supported infiltration by host fibroblasts and subsequent matrix remodeling. In conclusion, PGG-treated acellular pericardium is a promising scaffold for heart valve tissue engineering.

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Tannin interactions with a full‐length human salivary proline‐rich protein display a stronger affinity than with single proline‐rich repeats

Cited by 141 publications

References 15 publications

Interaction of Plant Polyphenols with Salivary Proteins

Interaction of Plant Polyphenols with Salivary Proteins

Molecular and thermodynamic basis for EGCG‐Keratin interaction‐part I: Molecular dynamics simulations

Stabilized Collagen Scaffolds for Heart Valve Tissue Engineering

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