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Study · In vitro (cell-free) · 2006

3 results

Zinc(II) binds to the neuroprotective peptide humanin.

Armas A, Sonois V, Mothes E, Mazarguil H, Faller P

Journal of inorganic biochemistry13 Jun 2006Cited by 37 (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

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

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

    Zn(II) and its substitutes Cd(II) and Co(II) bound to humanin through a thiolate bond from the side chain of the single cysteine at position 8.

    In plain wordsIn lab tests, zinc bound to humanin through its single cysteine amino acid.

    Peptide
    Humanin
    Outcome
    Not applicableZn(II) binding site on humanin
    Study

    n: not reported in source

    Metal-binding spectroscopy and titration in solution
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Zn(II) and its substitutes Cd(II)/Co(II) bind to humanin via a thiolate bond from the side chain of the single cysteine at position 8.
  2. 02LabIn vitro (cell-free)Activity measurement

    Titration experiments suggest that Zn(II) binds to humanin with an apparent affinity in the low micromolar range, similar to that for amyloid-beta and glutathione.

    In plain wordsIn lab tests, zinc bound humanin with an apparent affinity in the low micromolar range, similar to amyloid-beta and glutathione.

    Peptide
    Humanin
    Outcome
    Not applicableZn(II) binding affinity to humanin
    Study

    n: not reported in source

    Metal-binding spectroscopy and titration in solution
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Titration experiments suggest that Zn(II) binds to humanin with an apparent affinity in the low muM range.
    1 context sentence
    Summary · context
    This apparent Zn-binding affinity is in the same order as for amyloid-beta and glutathione and could thus be of physiological relevance.

Studies that did not test the peptide alone1

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

    The low intensity of the d-d bands of the Co(II)-humanin complex indicated an octahedral coordination geometry.

    In plain wordsIn lab tests, the cobalt-humanin complex had an octahedral shape.

    Peptide
    Humanin
    Outcome
    Not applicableCoordination geometry of Co(II)-humanin
    Study

    n: not reported in source

    Metal-binding spectroscopy and titration in solution
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    The low intensity of the d-d bands of Co(II)-humanin indicated an octahedral coordination geometry.

    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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