A hIAPP‐derived all‐d‐amino‐acid inhibits hIAPP fibrillation efficiently at membrane surface by targeting α‐helical oligomeric intermediates

A variety of peptides and peptide derivatives have been constructed using the “β‐sheet core segment” of amyloid proteins as inhibitors of amyloidogenic fibrillation. A novel all‐d‐amino‐acid from hIAPP β‐sheet core segment (hIAPP 22–27) is demonstrated to inhibit hIAPP fibril formation efficiently both at the phospholipid membrane and in bulk solution. The inhibitor terminates hIAPP aggregation to the α‐helical oligomeric intermediates at the membrane surface, whereas it stops the aggregation at the stage of β‐sheet oligomeric intermediates in bulk solution. This is the first evidence that the inhibition mechanism of the inhibitor at membrane surface is significantly different from that in bulk solution.

• Publication year

  2014

• Venue

  FEBS Letters

• Publication date

  2014-03-18

• Fields of study

  Medicine, Chemistry

• Identifiers
  DOI 10.1016/j.febslet.2014.02.020PMID 24561193
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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