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Study · Not a test of the peptide alone · 2008

4 results

The complex structure transition of Humanin peptides by sodium dodecylsulfate and trifluoroethanol.

Kita Y, Niikura T, Arisaka F, Arakawa T

Protein and peptide letters1 Jan 2008Cited by 6 (Europe PMC)

PMID18537742 (opens in a new tab)DOI10.2174/092986608784567555 (opens in a new tab)PepBankPUB-18537742
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 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)Other

    HNG and AGA-(C8R)HNG17 underwent complex conformational changes with increasing concentrations of SDS and TFE.

    In plain wordsIn lab tests, two Humanin analogs changed shape in complex ways when SDS or TFE was added.

    Peptide
    Humanin
    Outcome
    Not applicableConformational changes of HNG and AGA-(C8R)HNG17 with SDS and TFE
    Study

    n: not reported in source

    Outcome group
    Peptide structure and chemistry · Pharmacology

    Source sentences

    Summary
    Both HNG and AGA-(C8R)HNG17 underwent complex conformational changes with increasing concentrations of SDS and TFE, in contrast to general trend of increasing alpha-helix with their concentration.

    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

    Both peptides appeared to converge into a similar structure at higher SDS (above 0.05 %) and TFE (30-40 %) concentrations.

    In plain wordsIn lab tests, two Humanin analogs took on a similar shape at higher SDS and TFE concentrations.

    Peptide
    Humanin
    Outcome
    Not applicableConvergence of HNG and AGA-(C8R)HNG17 structures at high SDS and TFE
    Study

    n: not reported in source

    Outcome group
    Peptide structure and chemistry · Pharmacology

    Source sentences

    Summary
    To our surprise, both peptides appear to converge into a similar structure in SDS and TFE at higher concentrations; e.g., above 0.05 % SDS or 30-40 % TFE.

    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

    HNG at 0.1 mg/ml in PBS showed extensive aggregation without SDS but formed a highly homogeneous solution in 0.1 % SDS.

    In plain wordsIn lab tests, the Humanin analog HNG clumped in a salt buffer but stayed evenly dissolved when 0.1 % SDS was added.

    Peptide
    Humanin
    Outcome
    Not applicableAggregation of HNG in PBS and in SDS
    Study

    n: not reported in source

    Outcome group
    Peptide structure and chemistry · Pharmacology

    Source sentences

    Summary
    Sedimentation velocity analysis showed extensive aggregation of HNG at 0.1 mg/ml in PBS in the absence of SDS, but a highly homogeneous solution in 0.1 % SDS, indicating formation of a uniform structure by SDS.

    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

    HNG and AGA-(C8R)HNG17 formed an intermediate structure in SDS and TFE at lower concentrations, which appeared associated with extensive aggregation.

    In plain wordsIn lab tests, two Humanin analogs formed an in-between shape at low SDS and TFE levels, linked to clumping.

    Peptide
    Humanin
    Outcome
    Not applicableIntermediate structure of HNG and AGA-(C8R)HNG17 at low SDS and TFE
    Study

    n: not reported in source

    Outcome group
    Peptide structure and chemistry · Pharmacology

    Source sentences

    Summary
    These two peptides also formed an intermediate structure both in SDS and TFE at lower concentrations, which appeared to be associated with 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.

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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