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Ability of a salivary intrinsically unstructured protein to bind different tannin targets revealed by mass spectrometry

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Abstract

Astringency is thought to result from the interaction between salivary proline-rich proteins (PRP) that belong to the intrinsically unstructured protein group (IUP), and tannins, which are phenolic compounds. IUPs have the ability to bind several and/or different targets. At the same time, tannins have different chemical features reported to contribute to the sensation of astringency. The ability of both electrospray ionization mass spectrometry and tandem mass spectrometry to investigate the noncovalent interaction occurring between a human salivary PRP, IB5, and a model tannin, epigallocatechin 3-O-gallate (EgCG), has been reported. Herein, we extend this method to study the effect of tannin chemical features on their interaction with IB5. We used five model tannins, epigallocatechin (EgC), epicatechin 3-O-gallate (ECG), epigallocatechin 3-O-gallate (EgCG), procyanidin dimer B2 and B2 3′-O-gallate, which cover the main tannin chemical features: presence of a gallate moiety (galloylation), the degree of polymerization, and the degree of B ring hydroxylation. We show the ability of IB5 to bind these tannins. We report differences in stoichiometries and in stability of the IB5•1 tannin complexes. These results demonstrate the main role of hydroxyl groups in these interactions and show the involvement of hydrogen bonds. Finally, these results are in line with sensory analysis, by Vidal et al. (J Sci Food Agric 83:564–573, 2003) pointing out that the chain length and the level of galloylation are the main factors affecting astringency perception.

CID MS/MS approach to monitor the stability of noncovalent complexes between a human salivary proline-rich protein and model tannins that cover the main chemical features of tannins

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Abbreviations

CID:

Collision-induced dissociation

EgC:

Epigallocatechin

ECG:

Epicatechin gallate

EgCG:

Epigallocatechin gallate

B2 3′-OG:

B2 3′-O-gallate

ESI:

Electrospray ionization

IUP:

Intrinsically unstructured protein

MS:

Mass spectrometry

MS/MS:

Tandem mass spectrometry

PRP:

Proline-rich protein

bPRP:

Basic proline-rich protein

aPRP:

Acidic proline-rich protein

Q-TOF:

Quadrupole/time-of-flight

T:

Tannin

UGT:

Ungalloylated tannin

GT:

Galloylated tannin

M:

Monomer

GM:

Galloylated monomer

D:

Dimer

GD:

Galloylated dimer

DP:

Degree of polymerization

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Acknowledgments

The authors thank Dr. Véronique Cheynier for helpful scientific discussions, Thérèse Marlin for protein purification, Jean-Paul Mazauric for tannin purification and Emmanuelle Meudec for mass spectrometry assistance. Francis Canon was supported by a grant of French Ministry of Research. This work is supported by grant 07-BLAN-0279 from the French Agence Nationale de la Recherche (A.N.R.). We acknowledge synchrotron SOLEIL and thank all staff for assistance in using beamline DISCO. AG thanks ABSciex (Les Ullis, France) for the loan of the IonCooler Guide.

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Authors and Affiliations

  1. INRA, UMR 1083 Sciences Pour l’Oenologie, 2, place Viala, F-34060, Montpellier, France

    Francis Canon, Franck Paté & Pascale Sarni-Manchado

  2. DISCO Beamline, Synchrotron Soleil, l’Orme des Merisiers, 91192, Gif sur Yvette, France

    Alexandre Giuliani

  3. CEPIA, INRA, BP 71627, 44316, Nantes Cedex 3, France

    Alexandre Giuliani

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  1. Francis Canon
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  3. Franck Paté
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  4. Pascale Sarni-Manchado
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Correspondence to Pascale Sarni-Manchado.

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Canon, F., Giuliani, A., Paté, F. et al. Ability of a salivary intrinsically unstructured protein to bind different tannin targets revealed by mass spectrometry. Anal Bioanal Chem 398, 815–822 (2010). https://doi.org/10.1007/s00216-010-3997-9

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