Dual-Functional Antimicrobial and Low-Fouling Cellulose Coatings.

Surfaces contaminated with pathogens raise significant concerns due to their potential role in increasing the risk of disease transmission and subsequent infection. Existing surface coatings face several challenges that undermine their effectiveness and their broader applicability. These include the impact of surface topography on pathogen adhesion, which leads to biofouling, high production costs, scalability issues, as well as environmental concerns stemming from the utilization of toxic antifoulants and biocides.

Young rat microbiota extracts strongly inhibit fibrillation of α-synuclein and protect neuroblastoma cells and zebrafish against α-synuclein toxicity.

The clinical manifestations of Parkinson's disease (PD) are driven by aggregation of α-Synuclein (α-Syn) in the brain. However, there is increasing evidence that PD may be initiated in the gut and thence spread to the brain, eg, via the vagus nerve. Many studies link PD to changes in the gut microbiome, and bacterial amyloid has been shown to stimulate α-Syn aggregation.

Reverse engineering the Gut-Brain Axis and microbiome-metabolomics for symbiotic/pathogenic balance in neurodegenerative diseases.

Deciphering the molecular communications along the gut-brain axis can help in understanding the pathophysiology of neurodegenerative diseases and exploiting the gut microbiome for therapeutics. However, gut microbes and their metabolites have a multifaceted role in mediating both brain physiology and neurodegenerative pathology. There is a lack of understanding of how and when this role is tipped in neurodegenerative diseases and what are those contributing factors, both at local (gut) and distal (neuronal) levels, that drive this imbalance.

Alzheimer's Progenitor Amyloid-β Targets and Dissolves Microbial Amyloids and Impairs Biofilm Function.

Alzheimer's disease (AD) is a leading form of dementia where the presence of extra-neuronal plaques of Amyloid-β (Aβ) is a pathological hallmark. However, Aβ peptide is also observed in the intestinal tissues of AD patients and animal models. In this study, it is reported that Aβ monomers can target and disintegrate microbial amyloids of FapC and CsgA formed by opportunistic gut pathogens, Pseudomonas aeruginosa and Escherichia coli, explaining a potential role of Aβ in the gut-brain axis.

Structure Dependent Differential Modulation of Aβ Fibrillization by Selenadiazole-Based Inhibitors.

Misfolding and fibrillar aggregation of Aβ is a characteristic hallmark of Alzheimer's disease and primarily participates in neurodegenerative pathologies. There has been no breakthrough made in the therapeutic regime of Alzheimer's disease while the pharmacological interventions against Aβ are designed to sequester and clear Aβ burden from the neurological tissues. Based on the physiological relevance of Aβ, therapeutic approaches are required to inhibit and stabilize Aβ fibrillization, instead of cleaning it from the neurological system.