Polyphenols, astringency and proline-rich proteins.
Recent, NMR and precipitation, studies of molecular recognition of proline-rich proteins and peptides by plant polyphenols are described and rationalized. The action of polysaccharides and caseins in the moderation of the astringent response, which is engendered by polyphenols present in foodstuffs and beverages, is described. The possible influence of plant cell wall glycoproteins on the process of lignification is discussed in the light of the observed affinity of phenolic substrates for prolyl residues in protein structures.
Luck
G
G
Department of Chemistry, University of Sheffield, U.K.
Liao
H
H
Murray
N J
NJ
Grimmer
H R
HR
Warminski
E E
EE
Williamson
M P
MP
Lilley
T H
TH
Haslam
E
E
D000595:Amino Acid Sequence; D001252:Astringents / Q000737:chemistry*; D002364:Caseins / Q000737:chemistry; D011232:Chemical Precipitation; D005419:Flavonoids; D008031:Lignin / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D010636:Phenols / Q000737:chemistry*; D010944:Plants / Q000737:chemistry; D011108:Polymers / Q000737:chemistry*; D059808:Polyphenols; D011134:Polysaccharides / Q000737:chemistry; D055232:Proline-Rich Protein Domains; D013662:Tea
D001252:Astringents; D002364:Caseins; D005419:Flavonoids; D010455:Peptides; D010636:Phenols; D011108:Polymers; D059808:Polyphenols; D011134:Polysaccharides; D013662:Tea; D008031:Lignin