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Study · In vitro (cell-free) · 2019

6 results

The Mitochondrial Peptide Humanin Targets but Does Not Denature Amyloid Oligomers in Type II Diabetes.

Levine ZA, Teranishi K, Okada AK, Langen R, Shea JE

Journal of the American Chemical Society3 Sept 2019Cited by 17 (Europe PMC)

PMID31456396 (opens in a new tab)DOI10.1021/jacs.9b04995 (opens in a new tab)PepBankPUB-31456396
Publisher pagePubMedAsk about this study
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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 study6

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

  1. 01LabIn vitro (cell-free)Mechanism

    In ThT spectroscopy and electron microscopy, HNG did not deconstruct mature IAPP fibrils and oligomers.

    In plain wordsIn lab tests, HNG did not break down mature IAPP fibrils or oligomers.

    Peptide
    Humanin
    Outcome
    No significant changeDeconstruction of mature IAPP fibrils and oligomers by HNG
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Metabolic and weight
    Studied dose
    Dose not stated

    Source sentences

    Summary
    From ThT spectroscopy and electron microscopy, we found that HNG does not deconstruct mature IAPP fibrils and oligomers, consistent with the simulations and our proposed hypothesis.
    1 context sentence
    Summary · context
    To test this hypothesis, we carried out simulations and experiments to extract the dominant interactions between the S14G-HN mutant (HNG) and a diverse set of IAPP structures.
  2. 02Computer modelIn silicoMechanism

    In molecular dynamics simulations, HNG-IAPP heterodimers were 10 times more stable than IAPP homodimers.

    In plain wordsIn computer simulations, HNG paired with IAPP was 10 times more stable than IAPP paired with itself.

    Peptide
    Humanin
    Outcome
    Not applicableHNG-IAPP heterodimer stability versus IAPP homodimer
    Study

    n: not reported in source

    Comparator
    IAPP homodimers
    Outcome group
    Receptor activity and mechanism · Metabolic and weight
    Studied dose
    Dose not stated

    Measurements

    relative stability
    10 fold
    HNG-IAPP heterodimer vs IAPP homodimer

    Source sentences

    Summary
    Simulations also indicate that HNG-IAPP heterodimers are 10 times more stable than IAPP homodimers, which explains the substoichiometric ability of HNG to inhibit amyloid growth.
    1 context sentence
    Summary · context
    To test this hypothesis, we carried out simulations and experiments to extract the dominant interactions between the S14G-HN mutant (HNG) and a diverse set of IAPP structures.
  3. 03Computer modelIn silicoMechanism

    In simulations, HNG did not denature IAPP despite strong attraction.

    In plain wordsIn computer simulations, HNG did not unfold IAPP, even though it bound strongly to it.

    Peptide
    Humanin
    Outcome
    No significant changeHNG denaturation of IAPP
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Metabolic and weight
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Despite this strong attraction, HNG does not denature IAPP.
    1 context sentence
    Summary · context
    To test this hypothesis, we carried out simulations and experiments to extract the dominant interactions between the S14G-HN mutant (HNG) and a diverse set of IAPP structures.
  4. 04Computer modelIn silicoMechanism

    In simulations, HNG bound IAPP near the disordered NFGAIL motif and wedged between amyloidogenic fragments.

    In plain wordsIn computer simulations, HNG bound IAPP near the NFGAIL motif, between fragments that form amyloid.

    Peptide
    Humanin
    Outcome
    Not applicableHNG binding site on IAPP
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Metabolic and weight
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Instead, HNG binds IAPP near the disordered NFGAIL motif, wedging itself between amyloidogenic fragments.
    1 context sentence
    Summary · context
    To test this hypothesis, we carried out simulations and experiments to extract the dominant interactions between the S14G-HN mutant (HNG) and a diverse set of IAPP structures.
  5. 05Computer modelIn silicoMechanism

    In simulations, HNG shielding of NFGAIL-flanking fragments reduced the formation of parallel IAPP beta-sheets and later nucleation of mature fibrils.

    In plain wordsIn computer simulations, HNG shielding reduced IAPP beta-sheet formation and the start of mature amyloid fibrils.

    Peptide
    Humanin
    Outcome
    DecreaseFormation of parallel IAPP beta-sheets and nucleation of amyloid fibrils
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Metabolic and weight
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Shielding of NFGAIL-flanking fragments reduces the formation of parallel IAPP β-sheets and subsequent nucleation of mature amyloid fibrils.
    1 context sentence
    Summary · context
    To test this hypothesis, we carried out simulations and experiments to extract the dominant interactions between the S14G-HN mutant (HNG) and a diverse set of IAPP structures.

Studies that did not test the peptide alone1

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. 06Computer modelNot a test of Humanin aloneIn silicoMechanism

    Replica-exchange simulations suggested that mitochondrial-derived peptides cap the growth of IAPP amyloid oligomers.

    In plain wordsIn computer simulations, mitochondrial-derived peptides appeared to cap the growth of amyloid oligomers.

    Peptide
    Humanin
    Outcome
    Not applicableCapping of amyloid oligomer growth by mitochondrial-derived peptides
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Metabolic and weight

    Source sentences

    Summary
    Replica-exchange molecular dynamics suggests that MDPs cap the growth of amyloid oligomers.
    1 context sentence
    Summary · context
    To test this hypothesis, we carried out simulations and experiments to extract the dominant interactions between the S14G-HN mutant (HNG) and a diverse set of IAPP structures.

    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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