A Review of Pectin-Based Material for Applications in Water Treatment.

Climate change and water are inseparably connected. Extreme weather events cause water to become more scarce, polluted, and erratic than ever. Therefore, we urgently need to develop solutions to reduce water contamination. This review intends to demonstrate that pectin-based materials are an excellent route to detect and mitigate pollutants from water, with several benefits. Pectin is a biodegradable polymer, extractable from vegetables, and contains several hydroxyl and carboxyl groups that can easily interact with the contaminant ions. In addition, pectin-based materials can be prepared in different forms (films, hydrogels, or beads) and cross-linked with several agents to change their molecular structure. Consequently, the pectin-based adsorbents can be tuned to remove diverse pollutants. Here, we will summarize the existing water remediation technologies highlighting adsorption as the ideal method. Then, the focus will be on the chemical structure of pectin and, from a historical perspective, on its structure after applying different cross-linking methods. Finally, we will review the application of pectin as an adsorbent of water pollutants considering the pectin of low degree methoxylation.

The chaperonin CCT inhibits assembly of α-synuclein amyloid fibrils by a specific, conformation-dependent interaction.

The eukaryotic chaperonin CCT (chaperonin containing TCP-1) uses cavities built into its double-ring structure to encapsulate and to assist folding of a large subset of proteins. CCT can inhibit amyloid fibre assembly and toxicity of the polyQ extended mutant of huntingtin, the protein responsible for Huntington's disease. This raises the possibility that CCT modulates other amyloidopathies, a still-unaddressed question. We show here that CCT inhibits amyloid fibre assembly of α-synuclein A53T, one of the mutants responsible for Parkinson's disease. We evaluated fibrillation blockade in α-synuclein A53T deletion mutants and CCT interactions of full-length A53T in distinct oligomeric states to define an inhibition mechanism specific for α-synuclein. CCT interferes with fibre assembly by interaction of its CCTζ and CCTγ subunits with the A53T central hydrophobic region (NAC). This interaction is specific to NAC conformation, as it is produced once soluble α-synuclein A53T oligomers form and blocks the reaction before fibres begin to grow. Finally, we show that this association inhibits α-synuclein A53T oligomer toxicity in neuroblastoma cells. In summary, our results and those for huntingtin suggest that CCT is a general modulator of amyloidogenesis via a specific mechanism.