Interaction of tannin with human salivary proline-rich proteins.

Tannins are polyphenolic compounds, widely distributed in plant-based foods, which have harmful effects on animals including humans. Salivary proline-rich proteins (PRPs) may act as a defence against tannins by forming complexes with them and thereby preventing their interaction with other biological compounds and absorption from the intestinal canal. The aim here was to compare the ability of members of the family of human PRPs to form insoluble complexes with tannin and to assess the stability of such complexes under conditions similar to those in the alimentary tract. Basic PRPs (BPRPs), which have no other known biological functions, were very effective in forming insoluble complexes with both condensed tannin and tannic acid. Practically no tannin bound to acidic PRPs (APRPs) and glycosylated PRPs (GPRPs), suggesting that tannin in the diet would not affect their biological activities. There were only small differences in the tannin-precipitating ability of various BPRPs of different sizes or sequences, indicating that, although there is considerable phenotypic variation of PRPs, it is not likely to cause marked individual variation in tannin-binding ability. Tryptic digestion of an APRP led to a marked increase in tannin binding to the resulting proline-rich peptides, supporting observations in other studies that there may be an interaction between the proline-poor N-terminal and the proline-rich C-terminal regions in native APRPs, which inhibits the biological activities of the proteins. Deglycosylation of a GPRP also led to a dramatic increase in tannin-binding ability, showing that the carbohydrate side-chains prevent binding of tannin. Most of the condensed tannin-PRP complexes remained insoluble under conditions similar to those in the stomach and small intestine, supporting the proposal that PRPs act as a defence against tannin.