Abstract
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.
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This work was supported by a Japan Society for the Promotion of Science Grant-in-Aid for Scientific Research (C).
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Hayashi, K., Sasabe, J., Chiba, T. et al. d-Ser-containing humanin shows promotion of fibril formation. Amino Acids 42, 2293–2297 (2012). https://doi.org/10.1007/s00726-011-0971-6
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DOI: https://doi.org/10.1007/s00726-011-0971-6