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The acquired enamel pellicle (AEP) is a thin, acellular, and organic film that forms spontaneously on the tooth surface within seconds of exposure to saliva (Dawes et al., 1963). It is composed primarily of salivary proteins, glycoproteins, and lipids, including statherin, proline-rich proteins, mucins, and cystatins (Siqueira et al., 2012). The AEP serves a dual role in oral health: it acts as a protective barrier against acid-induced demineralization and provides lubrication to reduce wear, but it also provides specific receptors for the attachment of oral bacteria, initiating biofilm formation (Vitorino et al., 2007). In clinical dentistry, the AEP is a target for preventive therapies that aim to modify its composition to enhance acid resistance or inhibit the adhesion of cariogenic bacteria like Streptococcus mutans (Hannig & Hannig, 2009). Therapeutic agents such as fluoride, stannous ions, and casein-derived peptides interact with or incorporate into the pellicle to bolster its protective functions (Vacca-Smith & Bowen, 2000). Understanding the molecular dynamics of the AEP is crucial for developing next-generation oral care products designed to prevent dental caries, erosion, and periodontal diseases.
Modification of the protein film composition to inhibit pathogenic bacterial colonization, enhance calcium and phosphate retention for remineralization, and provide a physical semi-permeable barrier against acid-mediated demineralization.
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