Binding of condensed tannins to salivary proteins is supposed to be involved in their astringency. First, complexes arising from the interaction of saliva from two individuals and tannins were studied. Then interaction mixture models containing purified saliva proteins were developed. The highest polymerized tannins predominantly precipitated together with the salivary proteins. Electrophoresis of proteins in combination with thiolysis analysis of tannins indicated proline-rich protein (PRP)-polyphenol complexes in precipitated fractions and also in the soluble ones with individual differences. Individual salivas exhibiting different protein patterns were discriminated with regard to their ability to interact with tannins. From binding studies with purified classes of salivary proteins, interactions were shown to depend on the nature of the protein, in particular on their glycosylation state. For low concentrations of tannins, glycosylated PRIP-tannin interactions led to complexes that remained soluble, whereas those arising from nonglycosylated PRP-tannin interactions were precipitated. This finding could indicate that under physiological conditions, complexes involving glycosylated proteins maintain part of the lubrication of the oral cavity, whereas tannin trapping leads to a lower astringency perception