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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)
Author(s) -
Sun Yunxiang,
Kakinen Aleksandr,
Xing Yanting,
Faridi Pouya,
Nandakumar Aparna,
Purcell Anthony W.,
Davis Thomas P.,
Ke Pu Chun,
Ding Feng
Publication year - 2019
Publication title -
small
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.785
H-Index - 236
eISSN - 1613-6829
pISSN - 1613-6810
DOI - 10.1002/smll.201970093
Subject(s) - beta sheet , barrel (horology) , self assembly , monomer , helix (gastropod) , peptide , amyloid (mycology) , biophysics , chemistry , islet , biochemistry , materials science , polymer , diabetes mellitus , biology , organic chemistry , ecology , inorganic chemistry , snail , composite material , endocrinology
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.