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Study · In vitro (cell-free) · 2016

4 results

Solution NMR structure and inhibitory effect against amyloid-β fibrillation of Humanin containing a d-isomerized serine residue.

Alsanousi N, Sugiki T, Furuita K, So M, Lee YH, Fujiwara T, Kojima C

Biochemical and biophysical research communications25 Jun 2016Cited by 18 (Europe PMC)

Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study4

2 results from studies that gave the peptide. No result from this study comes from people.

  1. 01LabIn vitro (cell-free)Activity measurement

    In cell-free assays, Humanin d-Ser14 showed potent inhibitory activity against amyloid-β fibrillation.

    In plain wordsIn lab tests without cells, a humanin variant strongly blocked amyloid-β fibrils from forming.

    Peptide
    Humanin
    Outcome
    DecreaseInhibition of amyloid-β fibrillation
    Study

    n: not reported in source

    In vitro amyloid-β fibrillation assay
    Outcome group
    Neuroprotection · Nervous system and cognition
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Here we demonstrated that Humanin d-Ser14 exhibited potent inhibitory activity against fibrillation of amyloid-β and remarkably higher binding affinity for amyloid-β than that of the Humanin wild-type and S14G mutant.
  2. 02LabIn vitro (cell-free)Activity measurement

    In cell-free assays, Humanin d-Ser14 had higher binding affinity for amyloid-β than the humanin wild-type and the S14G mutant.

    In plain wordsIn lab tests without cells, a humanin variant bound amyloid-β more strongly than normal humanin and another mutant.

    Peptide
    Humanin
    Outcome
    IncreaseBinding affinity for amyloid-β
    Study

    n: not reported in source

    In vitro amyloid-β binding assay
    Comparator
    Humanin wild-type and S14G mutant
    Outcome group
    Receptor activity and mechanism · Nervous system and cognition
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Here we demonstrated that Humanin d-Ser14 exhibited potent inhibitory activity against fibrillation of amyloid-β and remarkably higher binding affinity for amyloid-β than that of the Humanin wild-type and S14G mutant.

Studies that did not test the peptide alone2

In this study, Humanin was a lab tool or a carrier, part of a mix, or the subject of a lab method. These results are not evidence about taking Humanin.

  1. 03LabNot a test of Humanin aloneIn vitro (cell-free)Mechanism

    By NMR, d-isomerization of the Ser14 residue enabled drastic conformational rearrangement of Humanin.

    In plain wordsIn lab structure studies, changing one amino acid to its mirror form drastically changed the shape of humanin.

    Peptide
    Humanin
    Outcome
    Not applicableSolution structure of Humanin d-Ser14
    Study

    n: not reported in source

    Solution NMR
    Outcome group
    Receptor activity and mechanism · Nervous system and cognition

    Source sentences

    Summary
    In addition, we determined the solution structure of Humanin d-Ser14 by nuclear magnetic resonance (NMR) and showed that d-isomerization of the Ser14 residue enables drastic conformational rearrangement of Humanin.

    In this study, Humanin was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Humanin.

  2. 04LabNot a test of Humanin aloneIn vitro (cell-free)Mechanism

    NMR identified an amyloid-β-binding site on Humanin d-Ser14 at atomic resolution.

    In plain wordsIn lab structure studies, researchers located the site on a humanin variant where amyloid-β binds.

    Peptide
    Humanin
    Outcome
    Not applicableAmyloid-β-binding site on Humanin d-Ser14
    Study

    n: not reported in source

    Solution NMR
    Outcome group
    Receptor activity and mechanism · Nervous system and cognition

    Source sentences

    Summary
    Furthermore, we identified an amyloid-β-binding site on Humanin d-Ser14 at atomic resolution by NMR.

    In this study, Humanin was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Humanin.

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  1. Version 2Current

    13 Oct 2026, 21:44 UTC

    Study results updated

  2. Version 1

    13 Oct 2026, 16:31 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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