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oai:gredos.usal.es:10366/1454662025-04-30T19:49:40Zcom_10366_4182com_10366_4055com_10366_3946com_10366_3823col_10366_4183

New Anthocyanin–Human Salivary Protein Complexes Ferrer-Gallego, Raúl Soares, Susana Rivas Gonzalo, Julián C. Mateus, Nuno Escribano Bailón, María Teresa de Freitas, Victor Salivary proteins Astringency Mass spectrometry Saturation-transfer difference [EN] The interaction between phenolic compounds and salivary proteins is considered the basis of the poorly understood phenomenon of astringency. Furthermore, this interaction is an important factor in relation to their bioavailability. In this work, interactions between anthocyanin and human salivary protein fraction were studied by mass spectrometry (MALDI-TOF-MS and FIA-ESI-MS) and saturation-transfer difference (STD) NMR spectroscopy. Anthocyanins were able to interact with saliva proteins. The dissociation constant (KD) between malvidin 3-glucoside and salivary proline-rich proteins was 1.92 mM for the hemiketal form (pH 3.4) and 1.83 mM for the flavylium cation (pH 1.0). New soluble complexes between these salivary proteins and malvidin 3-glucoside were identified for the first time. 2021-03-02T19:32:44Z 2021-03-02T19:32:44Z 2015 info:eu-repo/semantics/article Ferrer Gallego, R. [et al.] (2015) New Anthocyanin - Human Salivary Protein Complexes, Langmuir 31(30), pp. 8392-8401. doi:10.1021/acs.langmuir.5b01122 0743-7463 http://hdl.handle.net/10366/145466 10.1021/acs.langmuir.5b01122 1520-5827 eng https://doi.org/10.1021/acs.langmuir.5b01122 http://creativecommons.org/licenses/by-nc-nd/4.0/ info:eu-repo/semantics/openAccess Attribution-NonCommercial-NoDerivatives 4.0 Internacional