Peptide Self‐Assembly: Amyloid Self‐Assembly of hIAPP8‐20 via the Accumulation of Helical Oligomers, α‐Helix to β‐Sheet Transition, and Formation of β‐Barrel Intermediates (Small 18/2019)
Source abstract
Abstract
In article number 1805166, Pu Chun Ke, Feng Ding, and co-workers study the amyloid self-assembly of human islet amyloid polypeptide (hIAPP)8-20, a process associated with many neurodegenerative diseases and diabetes. The peptide is found to aggregate from monomers to nanofibrils via the accumulation of helical oligomers, α-helix to β-sheet transition, and formation of β-barrel intermediates that may interact with the cell membrane and cause leakage.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Supramolecular Self-Assembly in Materials · Alzheimer's disease research and treatments
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Affiliations
Department of Physics Ningbo University Ningbo 315211 China
Department of Physics and Astronomy Clemson University Clemson SC 29634 USA
ARC Centre of Excellence in Convergent Bio‐Nano Science and Technology Monash Institute of Pharmaceutical Sciences Monash University 381 Royal Parade Parkville VIC 3052 Australia
Infection and Immunity Program & Department of Biochemistry and Molecular Biology Biomedicine Discovery Institute Monash University Clayton VIC 3800 Australia
References
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