D-Ser-containing humanin shows promotion of fibril formation

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

doi:10.1007/s00726-011-0971-6

D-Ser-containing humanin shows promotion of fibril formation

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

Department of Pharmacology

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

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.

Original language	English
Pages (from-to)	2293-2297
Number of pages	5
Journal	Amino Acids
Volume	42
Issue number	6
DOIs	https://doi.org/10.1007/s00726-011-0971-6
Publication status	Published - 2012 Jun

Keywords

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

ASJC Scopus subject areas

Biochemistry
Clinical Biochemistry
Organic Chemistry

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10.1007/s00726-011-0971-6

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title = "D-Ser-containing humanin shows promotion of fibril formation",

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.",

keywords = "Circular dichroism, Humanin, d-Ser, α-Helix, β-Sheet",

author = "Kanehiro Hayashi and Jumpei Sasabe and Tomohiro Chiba and Sadakazu Aiso and Naoko Utsunomiya-Tate",

note = "Funding Information: This work was supported by a Japan Society for the Promotion of Science Grant-in-Aid for Scientific Research (C).",

year = "2012",

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doi = "10.1007/s00726-011-0971-6",

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AU - Hayashi, Kanehiro

AU - Sasabe, Jumpei

AU - Chiba, Tomohiro

AU - Aiso, Sadakazu

AU - Utsunomiya-Tate, Naoko

N1 - Funding Information: This work was supported by a Japan Society for the Promotion of Science Grant-in-Aid for Scientific Research (C).

PY - 2012/6

Y1 - 2012/6

N2 - 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.

AB - 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.

KW - Circular dichroism

KW - Humanin

KW - d-Ser

KW - α-Helix

KW - β-Sheet

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SN - 0939-4451

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EP - 2297

JO - Amino Acids

JF - Amino Acids

IS - 6

ER -

D-Ser-containing humanin shows promotion of fibril formation

Abstract

Keywords

ASJC Scopus subject areas

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