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Oral biofilm extracellular matrix proteins are a diverse group of proteins secreted by oral bacteria that constitute a significant portion of the extracellular polymeric substance (EPS) in dental plaque. These proteins, including enzymes like glucosyltransferases (Gtfs) and various adhesins (e.g., AgI/II), play a critical role in the structural integrity and biochemical environment of the biofilm (Bowen et al., 2018, JDR). They facilitate the adhesion of bacteria to the tooth surface and to each other, while also creating a protective barrier that limits the penetration of antimicrobial agents (Flemming et al., 2016, Nature Reviews Microbiology). In the context of dental caries and periodontal disease, these proteins are essential for the accumulation of pathogenic biofilms and the localized production of acids or inflammatory factors (Xiao et al., 2012, JDR). Targeting these proteins offers a therapeutic strategy to disrupt biofilm formation or enhance the efficacy of traditional antimicrobials without necessarily killing the bacteria, thereby reducing the selective pressure for antibiotic resistance (Koo et al., 2017, Nature Reviews Microbiology). Current research focuses on small molecule inhibitors of Gtfs and matrix-degrading enzymes to manage oral health more effectively.
Inhibition of glucosyltransferase (Gtf) and fructosyltransferase (Ftf) enzymes to prevent the synthesis of extracellular polysaccharides, enzymatic hydrolysis of existing matrix components (e.g., glucans), and competitive inhibition of adhesin-mediated bacterial binding to the salivary pellicle.
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