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Study · Not a test of the peptide alone · 2006

4 results

The secondary structure analysis of a potent Ser14Gly analog of antiAlzheimer peptide, Humanin, by circular dichroism.

Arakawa T, Niikura T, Tajima H, Kita Y

Journal of peptide science : an official publication of the European Peptide Society1 Oct 2006Cited by 19 (Europe PMC)

PMID16835886 (opens in a new tab)DOI10.1002/psc.773 (opens in a new tab)PepBankPUB-16835886
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

    By circular dichroism, the S14G analog of humanin had a more disordered secondary structure in water than in phosphate-buffered saline.

    In plain wordsIn lab tests, the S14G humanin analog was more disordered in water than in saline.

    Peptide
    Humanin
    Outcome
    Not applicableS14G-humanin secondary structure in water versus PBS
    Study

    n: not reported in source

    Circular dichroism in water and phosphate-buffered saline
    Comparator
    Water versus PBS
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    The secondary structure is more disordered in water than in phosphate-buffered saline (PBS).
    1 context sentence
    Summary · context
    The structure of a highly potent Ser14Gly analog of antiAlzheimer peptide, Humanin, was examined by circular dichroism (CD).

    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

    In water, the structure of the S14G analog of humanin depended little on peptide concentration or temperature.

    In plain wordsIn lab tests, the S14G humanin analog kept a similar shape in water at different concentrations and temperatures.

    Peptide
    Humanin
    Outcome
    Not applicableConcentration and temperature effect on structure in water
    Study

    n: not reported in source

    Circular dichroism in water and phosphate-buffered saline
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    The peptide structure in water is little dependent on both peptide concentration and temperature.

    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

    In phosphate-buffered saline the S14G analog structure differed from that in water, more at higher concentration and temperature, which appears to be due to self-association by hydrophobic interactions.

    In plain wordsIn lab tests, the S14G humanin analog changed shape in saline, probably because the peptide molecules stuck together.

    Peptide
    Humanin
    Outcome
    Not applicableStructure in PBS and self-association
    Study

    n: not reported in source

    Circular dichroism in water and phosphate-buffered saline
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    On the contrary, the peptide structure was significantly different in PBS from the structure in water, which is more apparent at a higher peptide concentration and temperature.
    1 context sentence
    Summary · context
    The observed different structure in PBS appears to be due to self-association of the peptide, which is enhanced by elevated temperature and, hence, via hydrophobic interactions.

    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

    Wild-type humanin also assumed a disordered structure in water and underwent conformational changes in phosphate-buffered saline.

    In plain wordsIn lab tests, wild-type humanin was disordered in water and changed shape in saline, like the S14G analog.

    Peptide
    Humanin
    Outcome
    Not applicableWild-type humanin structure in water versus PBS
    Study

    n: not reported in source

    Circular dichroism in water and phosphate-buffered saline
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    The wild-type Humanin also behaved similarly, i.e., it assumed a disordered structure in water but underwent conformational changes in PBS.

    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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