Literature DB >> 28225606

Effect of Astringent Stimuli on Salivary Protein Interactions Elucidated by Complementary Proteomics Approaches.

Judith Delius1, Guillaume Médard2, Bernhard Kuster2, Thomas Hofmann1.   

Abstract

The interaction of astringent substances with salivary proteins, which results in protein precipitation, is considered a key event in the molecular mechanism underlying the oral sensation of puckering astringency. As the chemical nature of orally active astringents is diverse and the knowledge of their interactions with salivary proteins rather fragmentary, human whole saliva samples were incubated with suprathreshold and isointensity solutions of the astringent polyphenol (-)-epigallocatechin gallate, the multivalent metal salt iron(III) sulfate, the amino-functionalized polysaccharide chitosan, and the basic protein lysozyme. After separation of the precipitated proteins, the proteins affected by the astringents were identified and relatively quantified for the first time by complementary bottom-up and top-down mass spectrometry-based proteomics approaches. Major salivary target proteins, which may be involved in astringency perception, are reported here for each astringent stimulus.

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Keywords:  astringency; chitosan; iBAQ; intensity-based absolute quantification; mass spectrometry; nano-LC-MS; oral cavity; polycation; polyphenol

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Year:  2017        PMID: 28225606     DOI: 10.1021/acs.jafc.7b00436

Source DB:  PubMed          Journal:  J Agric Food Chem        ISSN: 0021-8561            Impact factor:   5.279


  1 in total

1.  Label-free quantitative 1H NMR spectroscopy to study low-affinity ligand-protein interactions in solution: A contribution to the mechanism of polyphenol-mediated astringency.

Authors:  Judith Delius; Oliver Frank; Thomas Hofmann
Journal:  PLoS One       Date:  2017-09-08       Impact factor: 3.240

  1 in total

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