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Study · Not a test of the peptide alone · 2008

5 results

The structure analysis of Humanin analog, AGA-(C8R)HNG17, by circular dichroism and sedimentation equilibrium: comparison with the parent molecule.

Arisaka F, Niikura T, Arakawa T, Kita Y

International journal of biological macromolecules1 Apr 2008Cited by 12 (Europe PMC)

PMID18456318 (opens in a new tab)DOI10.1016/j.ijbiomac.2008.03.007 (opens in a new tab)PepBankPUB-18456318
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 study5

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

Studies that did not test the peptide alone5

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 (cells)Activity measurement

    A shorter 17-amino acid Humanin analog, AGA-(C8R)HNG17, was found to have 100-fold higher activity than HNG.

    In plain wordsIn lab tests, a shortened Humanin analog was 100 times more active than the analog HNG.

    Peptide
    Humanin
    Outcome
    IncreaseBiological activity of AGA-(C8R)HNG17 versus HNG
    Study

    n: not reported in source

    Comparator
    HNG
    Outcome group
    Neuroprotection · Nervous system and cognition

    Source sentences

    Summary
    During additional mutational analysis, a shorter 17-amino acid form, AGA-(C8R)HNG17, was accidentally discovered to have a 100-fold higher activity than HNG.

    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)Other

    The AGA-(C8R)HNG17 peptide exhibited extensive beta-sheet structure in water, unlike aqueous HN and HNG.

    In plain wordsIn lab tests, a Humanin analog formed a sheet-like structure in water, unlike Humanin and HNG.

    Peptide
    Humanin
    Outcome
    Not applicableSecondary structure of AGA-(C8R)HNG17 in water
    Study

    n: not reported in source

    Outcome group
    Peptide structure and chemistry · Pharmacology

    Source sentences

    Summary
    The AGA-(C8R)HNG17 peptide exhibited extensive beta-sheet structure in water, completely different from the aqueous HN and HNG 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.

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

    The beta-sheet structure of AGA-(C8R)HNG17 converted to a disordered structure in PBS at low peptide concentration, similar to HN and HNG.

    In plain wordsIn lab tests, the sheet-like structure of a Humanin analog became disordered in a salt buffer at low concentration.

    Peptide
    Humanin
    Outcome
    Not applicableStructure of AGA-(C8R)HNG17 in PBS at low concentration
    Study

    n: not reported in source

    Outcome group
    Peptide structure and chemistry · Pharmacology

    Source sentences

    Summary
    The beta-sheet structure was converted to a disordered structure upon dilution into phosphate-buffered saline (PBS) at low peptide concentration (e.g., below 0.2mg/ml), which was similar to the structure of HN and HNG, observed under similar conditions.

    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)Other

    AGA-(C8R)HNG17 was essentially monomeric in PBS, while HNG showed extensive aggregation.

    In plain wordsIn lab tests, the Humanin analog AGA-(C8R)HNG17 stayed single while HNG clumped together in a salt buffer.

    Peptide
    Humanin
    Outcome
    Not applicableAggregation of AGA-(C8R)HNG17 versus HNG in PBS
    Study

    n: not reported in source

    Comparator
    HNG
    Outcome group
    Peptide structure and chemistry · Pharmacology

    Source sentences

    Summary
    Sedimentation equilibrium analysis showed that the AGA-(C8R)HNG17 analog was essentially monomeric in PBS, while HNG showed extensive aggregation.

    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.

  5. 05LabNot a test of Humanin aloneIn vitro (cell-free)Other

    Aggregation of HNG was observed when the peptide was added to serum-containing cell culture media.

    In plain wordsIn lab tests, the Humanin analog HNG clumped together in cell culture fluid that contained serum.

    Peptide
    Humanin
    Outcome
    Not applicableAggregation of HNG in serum-containing cell culture media
    Study

    n: not reported in source

    Outcome group
    Peptide structure and chemistry · Pharmacology

    Source sentences

    Summary
    Such aggregation of HNG was observed when the peptide was added to the serum-containing cell culture media.

    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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