Bioinspired synthetic polymers-based inhibitors of Alzheimer's amyloid-β peptide aggregation

Rupali, .; Joseph, Blessy; Thomas, Sabu; Sen, Newton; Paschold, André; Binder, Wolfgang H.; Kumar, Sonu

doi:10.1039/d2py01217k

Cited by 4 publications

(4 citation statements)

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“…Some examples of diseases caused by protein aggregation include Alzheimer's, Parkinson's, type II diabetes, and prion diseases. [65][66][67][68][69][70] Amyloid fibrillation causing e. g. Alzheimer's or Parkinson's are generally seen as irreversible processes in in vivo conditions. Recently, the thermodynamics of amyloid fibril formation has been increasingly studied in vitro, which has shown that fibril formation is reversible under appropriate conditions.…”

Section: Protein Structure Folding and Misfoldingmentioning

confidence: 99%

“…Misfolded proteins sometimes can escape these checks, which can lead to protein aggregation, for example in the form of amyloid fibrils, resulting in disease. Some examples of diseases caused by protein aggregation include Alzheimer's, Parkinson's, type II diabetes, and prion diseases [65–70] . Amyloid fibrillation causing e .…”

Section: Proteinsmentioning

confidence: 99%

“…Synthetic polymers have also been applied as inhibitors of amyloid‐β peptide aggregation, responsible for Alzheimer's disease [66] . Many different polymeric designs have been reported so far, relying on targeted as well as aspecific interactions to prevent or disrupt amyloid aggregation.…”

Section: Folding Synthetic Polymers Into Functional Nanostructuresmentioning

confidence: 99%

“…Synthetic polymers have also been applied as inhibitors of amyloid-β peptide aggregation, responsible for Alzheimer's disease. [66] Many different polymeric designs have been reported so far, relying on targeted as well as aspecific interactions to prevent or disrupt amyloid aggregation. Of particular interest is the work by Binder and coworkers, who used polymers based on poly(ethylene oxide) acrylate and different hydrophobic end-groups for a specific hydrophilic/ hydrophobic ratio.…”

Section: Protein Stabilizationmentioning

confidence: 99%

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Protein‐Inspired Control over Synthetic Polymer Folding for Structured Functional Nanoparticles in Water

Wijker

Palmans

2023

ChemPlusChem

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The folding of proteins into functional nanoparticles with defined 3D structures has inspired chemists to create simple synthetic systems mimicking protein properties. The folding of polymers into nanoparticles in water proceeds via different strategies, resulting in the global compaction of the polymer chain. Herein, we review the different methods available to control the conformation of synthetic polymers and collapse/fold them into structured, functional nanoparticles, such as hydrophobic collapse, supramolecular self‐assembly, and covalent cross‐linking. A comparison is made between the design principles of protein folding to synthetic polymer folding and the formation of structured nanocompartments in water, highlighting similarities and differences in design and function. We also focus on the importance of structure for functional stability and diverse applications in complex media and cellular environments.

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