Polyphenol/Peptide Binding and Precipitation
University of Sheffield · Unilever (United Kingdom)
Abstract
Polyphenols are largely responsible for the astringency and "mouthfeel" of tea and wine by their interactions with basic salivary proline-rich proteins. Astringency arises from precipitation of polyphenol/peptide complexes, which is an important protective mechanism in animals that consume polyphenols. This paper presents biophysical studies of the interactions between chemically defined polyphenols and peptides. It is shown that intermolecular binding is dominated by stacking of polyphenolic rings onto planar hydrophobic surfaces and is strengthened by multiple cooperative binding of polyphenolic rings. Affinities weaken at higher temperatures and are unaffected by pH between pH 3.8 and 6.0. Measurements of…
Citation impact
- FWCI
- 19.14
- Percentile
- 100%
- References
- 39
Authors
7- AJAdrian J. CharltonCorresponding
University of Sheffield, Unilever (United Kingdom)
- NJNicola J. Baxter
Unilever (United Kingdom), University of Sheffield
- MKMahera Khan
Unilever (United Kingdom), University of Sheffield
- AJArthur J.G. Moir
Unilever (United Kingdom), University of Sheffield
- EHEdwin Haslam
University of Sheffield, Unilever (United Kingdom)
Topics & keywords
- Polyphenol
- Chemistry
- Peptide
- Dynamic light scattering
- Precipitation
- Biophysics
- Crystallography
- Nanoparticle