ArticleProceedings of the National Academy of Sciences of the United States of America2013
Coexistence of ribbon and helical fibrils originating from hIAPP(20-29) revealed by quantitative nanomechanical atomic force microscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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33 citing papers in PubMed, 112 citations in OpenAlex.
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- Experimental Insights into Conformational Ensembles of Assembled β-Sheet Peptides.ACS central science · 2023Article
- Statistics and topology of fluctuating ribbons.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Ultrasound-induced protein restructuring and ordered aggregation to form amyloid crystals.European biophysics journal : EBJ · 2022Article
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- Evolution of Conformation, Nanomechanics, and Infrared Nanospectroscopy of Single Amyloid Fibrils Converting into Microcrystals.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Article
- Interpenetrating Cubes in the X-ray Crystallographic Structure of a Peptide Derived from MedinJournal of the American Chemical Society · 2020Article
- Half a century of amyloids: past, present and future.Chemical Society reviews · 2020Review
- Calibration of T-shaped atomic force microscope cantilevers using the thermal noise method.The Review of scientific instruments · 2020Article
- Amyloid Evolution: Antiparallel Replaced by Parallel.Biophysical journal · 2020Article
- Pristine and Hydroxylated Fullerenes Prevent the Aggregation of Human Islet Amyloid Polypeptide and Display Different Inhibitory Mechanisms.Frontiers in chemistry · 2020Article
- Kinetic Control of Parallel versus Antiparallel Amyloid Aggregation via Shape of the Growing Aggregate.Scientific reports · 2019Article
- Single-Molecular Heteroamyloidosis of Human Islet Amyloid Polypeptide.Nano letters · 2019Article
- Article
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Authors and funding
13 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Uncontrolled misfolding of proteins leading to the formation of amyloid deposits is associated with more than 40 types of diseases, such as neurodegenerative diseases and type-2 diabetes. These irreversible amyloid fibrils typically assemble in distinct stages. Transitions among the various intermediate stages are the subject of many studies but are not yet fully elucidated. Here, we combine high-resolution atomic force microscopy and quantitative nanomechanical mapping to determine the self-assembled structures of the decapeptide hIAPP(20-29), which is considered to be the fibrillating core fragment of the human islet amyloid polypeptide (hIAPP) involved in type-2 diabetes. We successfully follow the evolution of hIAPP(20-29) nanostructures over time, calculate the average thickening speed of small ribbon-like structures, and provide evidence of the coexistence of ribbon and helical fibrils, highlighting a key step within the self-assembly model. In addition, the mutations of individual side chains of wide-type hIAPP(20-29) shift this balance and destabilize the helical fibrils sufficiently relative to the twisted ribbons to lead to their complete elimination. We combine atomic force microscopy structures, mechanical properties, and solid-state NMR structural information to build a molecular model containing β sheets in cross-β motifs as the basis of self-assembled amyloids.
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