Host and microbial proteins and glycoproteins of the skin, mucosa, and saliva

Host and microbial proteins and glycoproteins on the skin, mucosa, and in saliva constitute a broad array of molecular targets for topical antiseptic and antimicrobial agents. These include host-derived molecules such as salivary mucins, proline-rich proteins, and epithelial cell surface proteins, as well as microbial-derived proteins like Microbial Surface Components Recognizing Adhesive Matrix Molecules (MSCRAMMs) (Patel et al., 2023). The primary therapeutic relevance of these molecules lies in their ability to bind cationic drugs, such as chlorhexidine, through electrostatic interactions with anionic groups like carboxyl and phosphate groups (StatPearls, 2023). This binding facilitates "substantivity," a phenomenon where the drug is slowly released over several hours, maintaining a persistent antimicrobial environment on the tissue surface (Lim & Watt, 2020). While these interactions are essential for preventing infections and managing oral biofilms, the non-specific nature of this targeting can lead to adverse effects such as extrinsic staining of dental surfaces and altered taste perception (NIH, 2022).

Other names

Surface proteinsSalivary glycoproteinsMucosal proteinsMicrobial surface components recognizing adhesive matrix moleculesMSCRAMMsSalivary pellicle proteins

The mechanism involves non-specific electrostatic binding of cationic antiseptic agents to anionic sites on host and microbial proteins and glycoproteins, which leads to the disruption of microbial cell membranes and the creation of a drug reservoir for sustained antimicrobial activity, a property known as substantivity (StatPearls, 2023; Lim & Watt, 2020).