Coexistence of ribbon and helical fibrils originating from hIAPP(20-29) revealed by quantitative nanomechanical atomic force microscopy

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 110; no. 8; p. 2798
• Main Authors: Zhang, Shuai, Andreasen, Maria, Nielsen, Jakob T, Liu, Lei, Nielsen, Erik H, Song, Jie, Ji, Gang, Sun, Fei, Skrydstrup, Troels, Besenbacher, Flemming, Nielsen, Niels C, Otzen, Daniel E, Dong, Mingdong
• Format: Journal Article
• Language: English
• Published: United States 19.02.2013
• Subjects: Amyloid - chemistry; Amyloid - genetics; Humans; Islet Amyloid Polypeptide; Microscopy, Atomic Force - methods; Models, Molecular; Mutation; Nanotechnology; Nuclear Magnetic Resonance, Biomolecular; Peptide Fragments - chemistry; Peptide Fragments - genetics; Protein Conformation

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 intermed...