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Study · Not a test of the peptide alone · 2010

4 results

Structure changes of natively disordered Humanin in the presence of lipid.

Hirano A, Shiraki K, Niikura T, Arakawa T, Kita Y

International journal of biological macromolecules29 Jan 2010Cited by 5 (Europe PMC)

PMID20116397 (opens in a new tab)DOI10.1016/j.ijbiomac.2010.01.012 (opens in a new tab)PepBankPUB-20116397
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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 study4

No result from this study comes from a test of the peptide.

Studies that did not test the peptide alone4

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. 01LabNot a test of Humanin aloneIn vitro (cell-free)Mechanism

    Humanin changed into a beta-sheet structure at neutral pH with negatively charged DOPG liposomes, but not with neutral DOPC liposomes.

    In plain wordsIn lab tests, humanin folded into a sheet-like shape with negatively charged fat bubbles but not with neutral ones.

    Peptide
    Humanin
    Outcome
    Not applicableStructure change with DOPG liposome
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Humanin underwent a large structure change into a typical beta-sheet structure at neutral pH in the presence liposome made of a negatively charged 1,2-dioleoyl-sn-glycero-3-phosphoglycerol (DOPG), but not an electrically neutral 1,2-dioleoyl-sn-glycero-3-phosphatidylcholine (DOPC).
    1 context sentence
    Summary · context
    Here we have examined the structure in lipid environments, i.e., in the presence of liposome by circular dichroism.

    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. 02LabNot a test of Humanin aloneIn vitro (cell-free)Mechanism

    NaCl had no effect on the humanin structure in neutral solution or in the presence of DOPC liposome.

    In plain wordsIn lab tests, adding salt did not change the shape of humanin in plain solution or with neutral fat bubbles.

    Peptide
    Humanin
    Outcome
    No significant changeEffect of NaCl on humanin structure
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    No effect of NaCl on the Humanin structure was observed in neutral solution and in the presence of DOPC liposome.
    1 context sentence
    Summary · context
    Here we have examined the structure in lipid environments, i.e., in the presence of liposome by circular dichroism.

    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.

  3. 03LabNot a test of Humanin aloneIn vitro (cell-free)Mechanism

    Increasing temperature changed the humanin structure through aggregation.

    In plain wordsIn lab tests, raising the temperature changed the shape of humanin because it clumped together.

    Peptide
    Humanin
    Outcome
    Not applicableEffect of temperature on humanin structure
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Increasing temperature resulted in changes in the structure due to aggregation.
    1 context sentence
    Summary · context
    Here we have examined the structure in lipid environments, i.e., in the presence of liposome by circular dichroism.

    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.

  4. 04LabNot a test of Humanin aloneIn vitro (cell-free)Mechanism

    Humanin had a relatively stable structure against temperature in the presence of DOPG liposome, independent of NaCl.

    In plain wordsIn lab tests, humanin kept a fairly stable shape when heated in the presence of negatively charged fat bubbles.

    Peptide
    Humanin
    Outcome
    Not applicableTemperature stability with DOPG liposome
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    On the other hand, the effects of temperature on the Humanin structure showed that it has a relatively stable structure in the presence of DOPG liposome independent of the presence of NaCl.
    1 context sentence
    Summary · context
    Here we have examined the structure in lipid environments, i.e., in the presence of liposome by circular dichroism.

    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.

Publication types

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