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Study · Not a test of the peptide alone · 2010

4 results

beta-Sheet aggregation of kisspeptin-10 is stimulated by heparin but inhibited by amphiphiles.

Nielsen SB, Franzmann M, Basaiawmoit RV, Wimmer R, Mikkelsen JD, Otzen DE

Biopolymers1 Aug 2010Cited by 7 (Europe PMC)

PMID20301214 (opens in a new tab)DOI10.1002/bip.21434 (opens in a new tab)PepBankPUB-20301214
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, Kisspeptin-10 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 Kisspeptin-10.

  1. 01LabNot a test of Kisspeptin-10 aloneIn vitro (cell-free)Mechanism

    In cell-free solution, heparin induced kisspeptin to form beta-sheet rich amyloid aggregates at neutral (pH 7.0) and slightly acidic (pH 5.2) conditions.

    In plain wordsIn lab tests, heparin made kisspeptin clump into sheet-like fibre aggregates at neutral and slightly acidic pH.

    Peptide
    Kisspeptin-10
    Outcome
    IncreaseBeta-sheet aggregation with heparin at pH 7.0 and pH 5.2
    Study

    n: not reported in source

    Kisspeptin-10 in solution
    Outcome group
    Peptide structure and chemistry · Pharmacology

    Source sentences

    Summary
    Here we show that heparin induces kisspeptin to form beta-sheet rich amyloid aggregates both at neutral (pH 7.0) and slightly acidic (pH 5.2) conditions.

    In this study, Kisspeptin-10 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 Kisspeptin-10.

  2. 02LabNot a test of Kisspeptin-10 aloneIn vitro (cell-free)Mechanism

    In cell-free solution, heparin addition led to aggregation after a lag phase, irrespective of the time of heparin addition, indicating heparin is needed to form fibrillation nuclei.

    In plain wordsIn lab tests, kisspeptin clumped after a delay once heparin was added, whatever the time of addition.

    Peptide
    Kisspeptin-10
    Outcome
    Not applicableTiming of aggregation after heparin addition
    Study

    n: not reported in source

    Kisspeptin-10 in solution
    Outcome group
    Peptide structure and chemistry · Pharmacology

    Source sentences

    Summary
    Addition of heparin leads to aggregation after a certain lag phase, irrespective of the time of addition of heparin, indicating that heparin is needed to facilitate the formation of fibrillation nuclei.

    In this study, Kisspeptin-10 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 Kisspeptin-10.

  3. 03LabNot a test of Kisspeptin-10 aloneIn vitro (cell-free)Mechanism

    In cell-free solution, submicellar concentrations of zwitterionic and anionic surfactants completely inhibited kisspeptin aggregation.

    In plain wordsIn lab tests, small amounts of surfactants fully stopped kisspeptin from clumping.

    Peptide
    Kisspeptin-10
    Outcome
    DecreaseAggregation with zwitterionic and anionic surfactants
    Study

    n: not reported in source

    Kisspeptin-10 in solution
    Outcome group
    Peptide structure and chemistry · Pharmacology

    Source sentences

    Summary
    Aggregation is completely inhibited by submicellar concentrations of zwitterionic and anionic surfactants.

    In this study, Kisspeptin-10 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 Kisspeptin-10.

  4. 04LabNot a test of Kisspeptin-10 aloneIn vitro (cell-free)Mechanism

    In cell-free solution, NMR data did not indicate persistent kisspeptin structure in the presence of zwitterionic surfactant micelles.

    In plain wordsIn lab tests, NMR did not show a lasting kisspeptin structure in the presence of surfactant micelles.

    Peptide
    Kisspeptin-10
    Outcome
    No significant changePersistent structure by NMR in zwitterionic surfactant micelles
    Study

    n: not reported in source

    Kisspeptin-10 in solution
    Outcome group
    Peptide structure and chemistry · Pharmacology

    Source sentences

    Summary
    Unlike previous reports, our NMR data do not indicate persistent structure in the presence of zwitterionic surfactant micelles.

    In this study, Kisspeptin-10 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 Kisspeptin-10.

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

    10 Oct 2026, 09:43 UTC

    Study results updated

  2. Version 1

    9 Oct 2026, 03:04 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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