This thesis investigates the effects of astringent model compounds on salivary proteins in order to better understand the molecular principles behind oral astringency. Quantitative NMR spectroscopy suggested the presence of soluble protein−astringent complexes, whereas MS-based proteomics and electron microscopy indicated that astringents interact with surface-associated pellicle proteins. Tribological experiments revealed that cationic astringents diminish the lubricating properties of mucin-type glycoproteins. In conclusion, these diverse occurrences contribute to the formation of the rough and puckering astringent sensation.