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| - Structural Features of Procyanidin Interactions with SalivaryProteins
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| - Procyanidin dimers and trimer C1 were synthesized, whereas (−)-epicatechin O-gallate and B2−3‘ ‘-O-gallate were isolated from grape seeds. Human saliva was separated into two fractions. Oneof these was mainly α-amylase and the other mainly proline-rich proteins (PRPs). The procyanidincompounds were combined with each of the saliva protein fractions and with bovine serum albumin.The protein−polyphenol interactions were observed using nephelometry. (+)-Catechin had a highertannin specific activity (TSA) for PRPs than (−)-epicatechin (1.45 versus 0.65 nephelos turbidityunits/mg of polyphenol). This indicated the effect of the stereochemistry of flavan-3-ols on theirinteraction with proteins. Procyanidin dimers linked through a C(4)−C(8) interflavanoid bond hadconsistently greater TSA than their counterparts with a C(4)−C(6) linkage. Esterification of a galloylgroup to the C(3) hydroxyl function of (−)-epicatechin or to the epicatechin moiety of procyanidindimer B2 increased TSA. This was not as strong an effect for the dimer, probably as a result of theexpected “closed” structure of B2−3‘ ‘-O-gallate. Keywords: Astringency; nephelometry; grape seeds; procyanidin; salivary proteins; BSA
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