Fluoro-substituted cyanine for reliable in vivo labelling of amyloid-β oligomers and neuroprotection against amyloid-β induced toxicity† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c7sc03974c

Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization† †Electronic supplementary information (ESI) available: Experimental procedures, list of all the synthesized peptides and their % hIAPP fibrillization inhibition, MTT cytotoxicity assay, crystallization, details of X-ray structure determination, in silico docking of FGAΔFI with hIAPP, CD studies, Tables S1–S4, and Fig. S1–S6. CCDC 822015 and 904790. For ESI and crystallographic data in CIF or other electronic format see DOI: 10.1039/c3cc38982kClick here for additional data file. Click here for additional data file.

hIAPP fibrillization implicated in Type 2 diabetes pathology involves formation of oligomers toxic to insulin producing pancreatic β-cells. We report design, synthesis, 3D structure and functional characterization of dehydrophenylalanine (ΔF) containing peptides which inhibit hIAPP fibrillization. The inhibitor protects β-cells from hIAPP induced toxicity.

Decreasing amyloid toxicity through an increased rate of aggregation† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c6cp06765d. The data supporting the publication can be accessed at https://doi.org/10.17863/CAM.6653. Click here for additional data file.

Amyloid β is one of the peptides involved in the onset of Alzheimer's disease, yet the structure of the toxic species and its underlying mechanism remain elusive on account of the dynamic nature of the Aβ oligomerisation process. While it has been reported that incubation of Amyloid β (1-42) sequences (Aβ42) lead to formation of aggregates that vary in morphology and toxicity, we demonstrate th...

Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c7sc00620a Click here for additional data file.

Amyloid β-peptides 1–40 and 1–42 form oligomers with mixed β-sheets† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c7sc01743j

Two main amyloid-β peptides of different length (Aβ40 and Aβ42) are involved in Alzheimer's disease. Their relative abundance is decisive for the severity of the disease and mixed oligomers may contribute to the toxic species. However, little is know about the extent of mixing. To study whether Aβ40 and Aβ42 co-aggregate, we used Fourier transform infrared spectroscopy in combination with 13C-l...

Heparin acts as a structural component of β-endorphin amyloid fibrils rather than a simple aggregation promoter† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c6cc09770g Click here for additional data file.

The aggregation promoter heparin is commonly used to study the aggregation kinetics and biophysical properties of protein amyloids. However, the underlying mechanism for amyloid promotion by heparin remains poorly understood. In the case of the neuropeptide β-endorphin that can reversibly adopt a functional amyloid form in nature, aggregation in the presence of heparin leads to a loss of functi...