Schematic architecture of salivary conditioning films prior to and after chemical perturbation.

<p>(<b>A</b>) unperturbed salivary conditioning film, showing glycosylated mucins adsorbed in loops and trains over a layer of densely packed low-molecular weight proteins, including proline-rich proteins, histatins and lysozymes. (<b>B</b>) salivary conditioning film after exposure to detergents, showing removal of hydrophobic, smaller proteins and partial detachment of high molecular weight glycosylated mucins. Due to their larger size and multiple adsorption sites, larger proteins do not fully detach like the smaller ones. (<b>C</b>) salivary conditioning film after continued salivary flow over films exposed to detergents. Due to their smaller size, low molecular weight proteins adsorb faster than higher-molecular weight mucins, yielding a denser layer of adsorbed low-molecular weight proteins on the surface causing a greater structural softness and extended loops of glycosylated mucins, leaving the surface more hydrophilic. Smaller proteins have less chance to adsorb after exposure to SLS because more trains are left that occupy the substratum surface than after exposure to NaHMP.