This review focuses on the crucial role of aquatic ecosystems in preserving biodiversity and the biosphere, as well as the connection between antimicrobial resistance (AMR) and these ecosystems. It provides an in-depth analysis of the link between ecological well-being and public health, helping readers understand this complex subject. Aquatic ecosystems are essential for maintaining biodiversity and ecological balance. Additionally, they act as primary reservoirs and pathways for the spread of antimicrobial resistance (AMR). These ecosystems risk antibiotic contamination through various sources, such as the release of antibiotics from animal and human waste, improper disposal of unused medications, and pharmaceutical industry waste management practices. The presence of antibiotic residues in these environments significantly speeds up the development of bacterial resistance. The global prevalence of antimicrobial resistance (AMR) is evident in freshwater bodies, tributaries, sewage waters, and wastewater treatment facilities. Antimicrobial resistance (AMR) is now a significant public health threat, compromising the effectiveness of many previously successful treatments against various pathogens. One notable and alarming aspect of antimicrobial resistance (AMR) is its rapid development, often occurring within 5–10 years after introducing antimicrobial drugs to the market. This acceleration is closely tied to bacteria’s ability to thrive and adapt in the presence of antimicrobial agents and their residues in the environment. The implications of antimicrobial resistance (AMR) include treatment failures with long-term effects and a continuous increase in healthcare costs. This review comprehensively examines the intricate relationship between aquatic habitats, antibiotics, and the global challenge of antimicrobial resistance (AMR). It emphasizes the critical role of these ecosystems in preserving ecological diversity. It raises awareness about AMR’s urgent public health issue, laying a foundation for understanding its extensive consequences.

A series of 21 novel coumarin–triazole–isatin hybrids was synthesized and evaluated for their potential as multitarget agents in Alzheimer’s disease (AD). The compounds featured variations in alkyl linker length that connects coumarin and triazole and substitution at the 5-position of the isatin ring. Several derivatives showed potent butyrylcholinesterase (BChE) inhibition with selectivity over acetylcholinesterase (AChE). The lead compound, 6c1, exhibited strong BChE inhibition (IC₅₀ = 1.74 μM), surpassing donepezil. Enzyme kinetics revealed a mixed-type mechanism, while molecular docking studies confirmed dual binding at catalytic and peripheral sites. Structure–activity relationship (SAR) analysis highlighted the influence of linker flexibility and steric/electronic effects of substituents. The observed BChE selectivity, combined with favorable in vitro profiles, identifies these hybrids as promising leads for AD drug development.

Objective: Antibodies to ganglioside GM1 are associated with Guillain-Barré Syndrome (GBS) in patients with serologic evidence of a preceding infection with Campylobacter jejuni. Molecular mimicry between C. jejuni Lipopolysaccharide (LPS) and ganglioside GM1 has been proven to be the immunopathogenic mechanism of the disease in the axonal variant of GBS. GM1-positive sera cross-react with several Gal-GalNAc-bearing glycoproteins from the human peripheral nerve and C. jejuni (O:19). This study aimed to examine the immunoreactivity of the digested cross-reactive glycoproteins isolated from the human peripheral nerve and C. jejuni (O:19) with Peanut Agglutinin (PNA) as a marker for the Gal-GalNAc determinant, and with sera from patients with GBS. Materials and Methods: For this purpose, the cross-reactive glycoproteins from peripheral nerve and C. jejuni (O:19) were enzymatically digested with trypsin and the obtained peptides were incubated with PNA and GBS sera. Results: Western blot analysis of the separated peptides revealed several bands showing positive reactivity to PNA and to sera from patients with GBS, present in both digests from peripheral nerve and C. jejuni (O:19). Conclusions: These data indicate the possible molecular mimicry between the cross-reactive glycoproteins present in C. jejuni and human peripheral nerve and its potential role in the development of GBS following infection with C. jejuni (O:19).