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Microbial and viral membranes and structural proteins represent a broad class of therapeutic targets essential for the survival and pathogenicity of infectious agents. In bacteria, the cytoplasmic membrane and cell wall components, such as peptidoglycan, maintain osmotic pressure and provide a barrier against environmental stress (StatPearls, 2023). Viral structural proteins, including those forming the capsid or the lipid envelope, are vital for protecting the viral genome and mediating entry into host cells through specific binding and fusion events (Nature Reviews Microbiology, 2019). These components are the primary targets for various anti-infective drugs. For example, polymyxins and daptomycin target bacterial membranes to cause depolarization and cell death (PubMed, 2021), while polyene antifungals like amphotericin B bind to ergosterol in fungal membranes to form lethal pores (PubChem, 2024). Antiviral agents like enfuvirtide target structural proteins to inhibit viral-cell fusion (NIH, 2022). While these targets often provide high selectivity, therapeutic challenges include the emergence of drug resistance and potential toxicity to host cells. Notable safety concerns include the nephrotoxicity associated with membrane-disrupting agents (StatPearls, 2023). Overall, targeting these structural elements remains a cornerstone of anti-infective therapy despite the complexity of the target group.
Disruption of membrane integrity, pore formation, inhibition of cell wall synthesis, and blocking of viral fusion or assembly.
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