Interaction of Tannin with Human Salivary Histatins

Naurato, Nicholas; Wong, Pauline; Lu, Ying; Wróblewski, Karol; Bennick, Anders

doi:10.1021/jf981044i

Cited by 80 publications

(64 citation statements)

References 27 publications

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“…At a low concentration of condensed tannin or tannic acid, histatins were more readily precipitated from saliva than PRPs, and more condensed tannin and tannic acid were precipitated by histatin than gelatin at neutral pH, demonstrating the effectiveness of histatin in precipitating tannin. Further studies (Naurato et al ., 1999) indicated that Histatins 3 and 5 apparently share the same condensed tannin-binding region, which is located throughout the shared histatin 5 sequence, and they bound more condensed tannin than histatin 1. Epigallocatechin gallate (EGCG) showed binding characteristics similar to those of condensed tannin, while pentagalloyl glucose (PGG) bound equally well to histatins 1, 3, and 5.…”

Section: (Viii) Interaction Of Salivary Proteins and Tanninmentioning

confidence: 93%

Interaction of Plant Polyphenols with Salivary Proteins

Bennick

2002

Critical Reviews in Oral Biology & Medicine

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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: 93%

Interaction of Plant Polyphenols with Salivary Proteins

Bennick

2002

Critical Reviews in Oral Biology & Medicine

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385

265

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“…Similarly, the profisetinidin CTs from quebracho interacted with salivary histatins by a different mode than PGG. 246 Although it has been known for some time that the binding strengths in different tannin-protein complexes can vary over orders of magnitude, 87 surprisingly few studies have related the protein-binding abilities of tannins to in vivo protein digestibilities. Robbins et al 143 concluded that the reduction in protein digestibility in wild ruminants was proportional to the BSA protein-precipitating capacity of plant tannins.…”

Section: Protein Precipitation Assaysmentioning

confidence: 99%

Unravelling the conundrum of tannins in animal nutrition and health

2006

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This paper examines the nutritional and veterinary effects of tannins on ruminants and makes some comparisons with non-ruminants. Tannin chemistry per se is not covered and readers are referred to several excellent reviews instead: (a) Okuda T et al. Heterocycles 30:1195-1218 (1990); (b) Ferreira D and Slade D. Nat Prod Rep 19:517-541 (2002); (c) Yoshida T et al. In Studies in Natural Product Chemistry. Elsevier Science, Amsterdam, pp. 395-453 (2000); (d) Khanbabaee K and van Ree T. Nat Prod Rep 18:641-649 (2001); (e) Okuda et al. Phytochemistry 55:513-529 (2000). The effects of tannins on rumen micro-organisms are also not reviewed, as these have been addressed by others: (a) McSweeney CS et al. Anim Feed Sci Technol 91:83-93 (2001); (b) Smith AH and Mackie RI. Appl Environ Microbiol 70:1104-1115 (2004). This paper deals first with the nutritional effects of tannins in animal feeds, their qualitative and quantitative diversity, and the implications of tannin-protein complexation. It then summarises the known physiological and harmful effects and discusses the equivocal evidence of the bioavailability of tannins. Issues concerning tannin metabolism and systemic effects are also considered.Opportunities are presented on how to treat feeds with high tannin contents, and some lesser-known but successful feeding strategies are highlighted. Recent research has explored the use of tannins for preventing animal deaths from bloat, for reducing intestinal parasites and for lowering gaseous ammonia and methane emissions. Finally, several tannin assays and a hypothesis are discussed that merit further investigation in order to assess their suitability for predicting animal responses. The aim is to provoke discussion and spur readers into new approaches. An attempt is made to synthesise the emerging information for relating tannin structures with their activities. Although many plants with high levels of tannins produce negative effects and require treatments, others are very useful animal feeds. Our ability to predict whether tannin-containing feeds confer positive or negative effects will depend on interdisciplinary research between animal nutritionists and plant chemists. The elucidation of tannin structure-activity relationships presents exciting opportunities for future feeding strategies that will benefit ruminants and the environment within the contexts of extensive, semi-intensive and some intensive agricultural systems.

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“…Several studies report the role of salivary PRPs and HRPs in binding phenolic compounds [2,3,5,7,9,29], therefore the focus here is directed toward the binding to a-amylase. Saliva amylase contains 22 proline and 16 tryptophan amino acid residues in its sequence (NCBI Protein data bank).…”

Section: Tryptophan Quenching Experimentsmentioning

confidence: 99%

Determining the binding affinities of phenolic compounds to proteins by quenching of the intrinsic tryptophan fluorescence

Rawel

Frey

Meidtner

et al. 2006

Mol. Nutr. Food Res.

129

100

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The noncovalent binding of selected phenolic compounds (chlorogenic-, ferulic-, gallic acid, quercetin, rutin, and isoquercetin) to proteins (HSA, BSA, soy glycinin, and lysozyme) was studied by an indirect method applying the quenching of intrinsic tryptophan fluorescence. From the data obtained, the binding constants were calculated by nonlinear regression (one site binding; y = Bx/k + x). It has been reported that tannins inhibit human salivary amylase and that these complexes may reduce the development of cariogenic plaques. Further, amylase contains two tryptophan residues in its active site. Therefore, in a second part of the study involving 31 human subjects, evidence was sought for noncovalent interactions between the phenols of green tea and saliva proteins as measured by the fluorescence intensity. Amylase activity was determined before and after the addition of green tea to saliva of 31 subjects. Forty percent of the subjects showed an increase in amylase activity contrary to studies reporting only a decrease in activity. The interactions of tannin with amylase result in a decrease of its activity. It still remains to be elucidated why amylase does not react uniformly under conditions of applying green tea to saliva. Further, in terms of using phenols as caries inhibitors this finding should be of importance.

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Interaction of Tannin with Human Salivary Histatins

Cited by 80 publications

References 27 publications

Interaction of Plant Polyphenols with Salivary Proteins

Interaction of Plant Polyphenols with Salivary Proteins

Unravelling the conundrum of tannins in animal nutrition and health

Determining the binding affinities of phenolic compounds to proteins by quenching of the intrinsic tryptophan fluorescence

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