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The dental biofilm matrix and pellicle proteins represent a complex assembly of host-derived salivary proteins and microbially produced extracellular substances that coat the tooth surface and provide the structural framework for dental plaque. The acquired enamel pellicle (AEP), formed within seconds of tooth cleaning, consists of proteins such as mucins (MUC5B, MUC7), statherin, and proline-rich proteins, which serve as the initial interface for bacterial colonization [Siqueira et al., 2012]. As the biofilm matures, bacteria like Streptococcus mutans secrete extracellular polymeric substances (EPS), including glucans and matrix proteins, which protect the microbial community from environmental stressors and antimicrobial agents [Koo et al., 2013]. This matrix is a critical therapeutic target because its disruption can prevent the formation of pathogenic biofilms associated with dental caries and periodontal disease [Bowen et al., 2018]. Drugs targeting this complex often work by inhibiting bacterial adhesion, degrading matrix components via enzymes like dextranase, or altering the chemical properties of the pellicle to reduce microbial affinity [Marsh, 2010].
Inhibition of bacterial adhesion to salivary pellicle proteins, enzymatic degradation of extracellular polymeric substances (EPS), and modification of the tooth surface charge to prevent biofilm accumulation [Koo et al., 2013; Marsh, 2010].
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