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Study · In vitro (cell-free) · 2005

4 results

Peptide-lipid interaction monitored by spin labeled biologically active melanocortin peptides.

Fernandez RM, Vieira RF, Nakaie CR, Ito AS, Lamy MT

Peptides1 Oct 2005Cited by 5 (Europe PMC)

PMID16006009 (opens in a new tab)DOI10.1016/j.peptides.2004.12.030 (opens in a new tab)PepBankPUB-16006009
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

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

  1. 01LabIn vitro (cell-free)Mechanism

    In lipid bilayers, electron spin resonance of Toac-labelled alpha-MSH and NDP-MSH indicated that both peptides insert into the bilayer close to its surface, in rather similar environments.

    In plain wordsIn lab tests, NDP-MSH and alpha-MSH both entered a lipid layer close to its surface.

    Peptide
    Melanotan I (afamelanotide)
    Outcome
    Not applicableInsertion of NDP-MSH into lipid bilayers
    Study

    n: not reported in source

    lipid bilayers
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    The Toac0 ESR of the membrane-bound peptides indicates that the two peptides are inserted into the bilayer, close to the bilayer surface, in rather similar environments.
    1 context sentence
    Summary · context
    The present work comparatively analyzes the interaction of alpha-MSH and its more potent and long-acting analog [Nle4, D-Phe7]alpha-MSH (NDP-MSH) with lipid bilayers.
  2. 02LabIn vitro (cell-free)Mechanism

    In lipid bilayers, Trp9 time-resolved fluorescence indicated that alpha-MSH, NDP-MSH and their Toac-labelled derivatives have rather similar membrane-bound conformations.

    In plain wordsIn lab tests, NDP-MSH and alpha-MSH had rather similar shapes when bound to a lipid layer.

    Peptide
    Melanotan I (afamelanotide)
    Outcome
    Not applicableMembrane-bound conformation of NDP-MSH compared with alpha-MSH
    Study

    n: not reported in source

    lipid bilayers
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Trp9 time resolved fluorescence indicates that the peptides, and their Toac-labeled derivatives, present rather similar conformations when membrane bound, though Trp9 in NDP-MSH, and in its Toac-labeled derivative, goes somewhat further down into the bilayer.
    1 context sentence
    Summary · context
    The present work comparatively analyzes the interaction of alpha-MSH and its more potent and long-acting analog [Nle4, D-Phe7]alpha-MSH (NDP-MSH) with lipid bilayers.
  3. 03LabIn vitro (cell-free)Mechanism

    In lipid bilayers, Trp9 of NDP-MSH went somewhat further down into the bilayer than Trp9 of alpha-MSH.

    In plain wordsIn lab tests, part of NDP-MSH went a little deeper into a lipid layer than the same part of alpha-MSH.

    Peptide
    Melanotan I (afamelanotide)
    Outcome
    Not applicableDepth of Trp9 in the bilayer
    Study

    n: not reported in source

    lipid bilayers
    Comparator
    alpha-MSH
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    though Trp9 in NDP-MSH, and in its Toac-labeled derivative, goes somewhat further down into the bilayer.
    1 context sentence
    Summary · context
    The present work comparatively analyzes the interaction of alpha-MSH and its more potent and long-acting analog [Nle4, D-Phe7]alpha-MSH (NDP-MSH) with lipid bilayers.
  4. 04LabIn vitro (cell-free)Mechanism

    In lipid bilayers, the Toac-labelled N-terminus of NDP-MSH sat in a shallower position in the bilayer than the Toac-labelled N-terminus of alpha-MSH.

    In plain wordsIn lab tests, the labelled front end of NDP-MSH sat closer to the surface of a lipid layer than that of alpha-MSH.

    Peptide
    Melanotan I (afamelanotide)
    Outcome
    Not applicableDepth of Toac-labelled N-terminus in the bilayer
    Study

    n: not reported in source

    lipid bilayers
    Comparator
    alpha-MSH
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Yet, Toac0 ESR signal shows that the Toac-labeled N-terminal of NDP-MSH is in a shallower position in the bilayer, as compared to the hormone.
    1 context sentence
    Summary · context
    The present work comparatively analyzes the interaction of alpha-MSH and its more potent and long-acting analog [Nle4, D-Phe7]alpha-MSH (NDP-MSH) with lipid bilayers.

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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