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Amyloids

Amyloids is a collective term to describe misfolded proteins that self-assemble into insoluble fibrils both in vitro and in vivo. These protein aggregates are involved in a wide variety of human diseases, from Alzheimer's Disease to Type 2 Diabetes and Rheumatoid Arthritis to Artherosclerosis. Given the importance of amyloids in a disease context, intense study of their biophysical properties has given plenty of new information on ways to inhibit their formation.

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Insight into the Interactions of Amyloid β-Sheets with Graphene Flakes: Scrutinizing the Role of Aromatic Residues in Amyloids that Interact with Graphene

Insight into the Interactions of Amyloid β‐Sheets with Graphene Flakes: Scrutinizing the Role of Aromatic Residues in Amyloids that Interact with Graphene

β-Amyloid peptide accumulation in the brain is most likely cause of the Alzheimer's disease. Aggregates of β-sheets of amyloid structures with a graphene flake (see picture) were studied by using DFT calculations. Graphene-flake interactions with amyloid sheets are stronger than the interaction between two amyloid sheets, which confirms experimental observations that graphene inhibits amyloid aggregation.

[Article]
Dragana M. Božinovski, Predrag V. Petrović, Milivoj R. Belić, Snežana D. Zarić
ChemPhysChem, December 13, 2017, https://doi.org/10.1002/cphc.201700847 Read article

A Small Molecule Impedes Insulin Fibrillation: Another New Role of Phenothiazine Derivatives

A Small Molecule Impedes Insulin Fibrillation: Another New Role of Phenothiazine Derivatives

Arrested aggregation: Protein misfolding is interrelated to several diseases, including neurodegenerative diseases and type II diabetes. Misfolded/unfolded proteins produce soluble oligomers that accumulate into “amyloid plaques”. Inhibition of amyloid-plaque formation by those misfolded proteins will lead to the invention of new therapeutic approaches for amyloid-related diseases. Herein, methylene blue (MB) is used to impede insulin fibrillation.

[Full Paper]
Meghomukta Mukherjee, Jagannath Jana, Subhrangsu Chatterjee
ChemistryOpen, December 07, 2017, https://doi.org/10.1002/open.201700131 Read article

Layer-by-Layer Assembly of κ-Casein Amyloid Fibrils for the Preparation of Hollow Microcapsules

Layer‐by‐Layer Assembly of κ‐Casein Amyloid Fibrils for the Preparation of Hollow Microcapsules

The growth and surface morphology of the layer-by-layer-assembled films are explored, consisting of zwitterionic κ-casein amyloid fibrils (κCF) depending on the types of intermolecular interactions. Stable and mechanically robust κCF/poly(sodium 4-styrenesulfonate) hollow microcapsules are only possible with the electrostatic interactions, while κCF/poly(acrylic acid) samples are ruptured due to the breakage of hydrogen bonding during the removal of sacrificial templates.

[Full Paper]
Jubong Lee, Ji-Hye Lee, Bongjun Yeom, Kookheon Char
Macromol. Chem. Phys., November 09, 2017, https://doi.org/10.1002/macp.201700382 Read article

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