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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...
The self‐assembly of human islet amyloid polypeptide (hIAPP) into β‐sheet‐rich nanofibrils is associated with the pathogeny of type 2 diabetes. Soluble hIAPP is intrinsically disordered with N‐terminal residues 8–17 as α‐helices. To understand the contribution of the N‐terminal helix to the aggregation of full‐length hIAPP, here the oligomerization dynamics of the hIAPP fragment 8–20 (hIAPP8‐20) are...
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