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Bacterial membrane thiol-containing proteins and lipids are essential components of the bacterial cell envelope and metabolic machinery, serving as critical targets for various antimicrobial agents (Jung et al., 2008, Applied and Environmental Microbiology). These molecules contain sulfhydryl (-SH) groups that are vital for maintaining the tertiary structure of proteins and the catalytic activity of enzymes involved in cellular respiration and nutrient transport (Russell & Hugo, 1994, Progress in Medicinal Chemistry). Antimicrobial agents, particularly silver ions (Ag+), exhibit a high affinity for these sulfur atoms, forming stable S-metal bonds that displace hydrogen ions. This interaction leads to the denaturation of membrane-bound proteins and the inactivation of essential enzymes, resulting in a loss of membrane potential and structural integrity (Slavin et al., 2017, Nanomaterials). The subsequent disruption of the bacterial respiratory chain and increased membrane permeability ultimately lead to cell death. Because these thiol groups are ubiquitous across many bacterial species, agents targeting them often possess broad-spectrum activity. However, the therapeutic use of such agents is often limited to topical applications or medical device coatings due to potential cross-reactivity with host thiol-containing proteins (Lansdown, 2002, Journal of Wound Care).
Covalent binding to and oxidation of sulfhydryl (thiol) groups, leading to protein denaturation and enzymatic inactivation.
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