D-Ser-containing humanin shows promotion of fibril formation

Kanehiro Hayashi, Jumpei Sasabe, Tomohiro Chiba, Sadakazu Aiso, Naoko Utsunomiya-Tate

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


Humanin (HN), a peptide of 24 amino acid residues, suppresses the neuronal cell death that is induced by the gene products of Alzheimer's disease. HN contains two Ser residues at positions 7 and 14. Because the proportion of d-Ser isomerized from l-Ser in proteins appears to increase as cellular organs age, we explored the structural effects of the isomerization of each Ser residue in HN. By using a thioflavin-T assay to detect fibril formation, we found that an HN derivative that contained two isomerized d-Ser residues had a greater tendency to form fibrils than did wild-type HN or HNs containing single d-Ser residues. A previous report showed that HN containing two d-Ser residues exerts neuroprotective activity. Our data, therefore, suggest that the fibril formation by HN that contains two d-Ser residues may promote HN neuroprotective activity.

Original languageEnglish
Pages (from-to)2293-2297
Number of pages5
JournalAmino Acids
Issue number6
Publication statusPublished - 2012 Jun
Externally publishedYes


  • Circular dichroism
  • Humanin
  • d-Ser
  • α-Helix
  • β-Sheet

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Organic Chemistry


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