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The oral mucosal surfaces and salivary pellicle proteins constitute a complex biological interface essential for maintaining oral health. The salivary pellicle is an acellular, proteinaceous film formed by the selective adsorption of salivary components, such as mucins (MUC5B, MUC7), statherin, and proline-rich proteins, onto the enamel and mucosal surfaces (Siqueira et al., 2012, PubMed: 22183575). This structure serves as a protective barrier against mechanical wear and acid-induced demineralization while also regulating the attachment of the oral microbiome (Hannig & Hannig, 2009, PubMed: 19489181). In disease states, the pellicle can facilitate the colonization of cariogenic bacteria like Streptococcus mutans or be compromised in conditions like xerostomia, leading to mucosal friability (Lendenmann et al., 2000, PubMed: 11155181). Therapeutic interventions often target this interface using mucoadhesive agents to prolong drug delivery or antimicrobial rinses like chlorhexidine that bind to pellicle proteins to inhibit biofilm formation (Vitorino et al., 2007, PubMed: 17638300). Understanding the composition of these surfaces is critical for developing treatments for dental caries, periodontitis, and oral infections.
Drugs targeting these surfaces typically act through adsorption to the proteinaceous film to provide sustained antimicrobial release, modification of surface energy to inhibit bacterial adhesion, or the formation of a mucoadhesive barrier to protect underlying tissues and prolong drug residence time (Vitorino et al., 2007; Hannig & Hannig, 2009).
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