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Study · In vitro (cell-free) · 2012

3 results

Interaction structure of the complex between neuroprotective factor humanin and Alzheimer's β-amyloid peptide revealed by affinity mass spectrometry and molecular modeling.

Maftei M, Tian X, Manea M, Exner TE, Schwanzar D, von Arnim CA, Przybylski M

Journal of peptide science : an official publication of the European Peptide Society20 Apr 2012Cited by 33 (Europe PMC)

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 study3

1 result from studies that gave the peptide. No result from this study comes from people.

  1. 01LabIn vitro (cell-free)Activity measurement

    Bioaffinity analysis with a surface acoustic wave biosensor gave a KD of 610 nm for the humanin and amyloid-beta(1-40) complex.

    In plain wordsIn lab tests, humanin bound amyloid-beta with a measured binding constant of 610 nm.

    Peptide
    Humanin
    Outcome
    Not applicableBinding affinity (KD) of humanin to amyloid-beta(1-40)
    Study

    n: not reported in source

    Synthetic peptides, affinity mass spectrometry
    Outcome group
    Receptor activity and mechanism · Nervous system and cognition
    Studied dose
    Dose not stated

    Measurements

    KD
    610 nm
    HN-Aβ(1-40) complex

    Source sentences

    Summary
    The specificity and affinity of the HN-Aß interaction were characterized by direct ESI-MS of the HN-Aß(1-40) complex and by bioaffinity analysis using a surface acoustic wave biosensor, providing a K(D) of the complex of 610 nm.
    1 context sentence
    Summary · context
    We report here the identification of the binding epitopes between HN and Aß(1-40) and characterization of the interaction structure through a molecular modeling study.

Studies that did not test the peptide alone2

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

    By affinity mass spectrometry, HN(5-15) was the humanin epitope and Aß(17-28) was the amyloid-beta interaction epitope in the HN-Aß(1-40) complex.

    In plain wordsIn lab tests, the parts of humanin and of amyloid-beta that bind each other were identified.

    Peptide
    Humanin
    Outcome
    Not applicableBinding epitopes of humanin and amyloid-beta(1-40)
    Study

    n: not reported in source

    Synthetic peptides, affinity mass spectrometry
    Outcome group
    Receptor activity and mechanism · Nervous system and cognition

    Source sentences

    Summary
    The affinity-MS analyses revealed HN(5-15) as the epitope sequence of HN, whereas Aß(17-28) was identified as the Aß interaction epitope.
    1 context sentence
    Summary · context
    We report here the identification of the binding epitopes between HN and Aß(1-40) and characterization of the interaction structure through a molecular modeling study.

    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. 03Computer modelNot a test of Humanin aloneIn silicoMechanism

    A molecular dynamics simulation of the HN-Aß(1-40) complex was consistent with the binding specificity and shielding effects of the interaction epitopes.

    In plain wordsIn a computer simulation, the humanin and amyloid-beta complex matched the binding sites found in the lab tests.

    Peptide
    Humanin
    Outcome
    Not applicableMolecular dynamics of the humanin and amyloid-beta(1-40) complex
    Study

    n: not reported in source

    Molecular dynamics simulation
    Outcome group
    Receptor activity and mechanism · Nervous system and cognition

    Source sentences

    Summary
    A molecular dynamics simulation of the HN-Aß(1-40) complex was consistent with the binding specificity and shielding effects of the HN and Aß interaction epitopes.
    1 context sentence
    Summary · context
    We report here the identification of the binding epitopes between HN and Aß(1-40) and characterization of the interaction structure through a molecular modeling study.

    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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