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Related Experiment Videos

des-(1-13) human beta-endorphin interacts with calmodulin.

D Puett, D P Giedroc, S Tollefson

    Peptides
    |March 1, 1983
    PubMed
    Summary

    A synthetic beta-endorphin fragment inhibits cyclic nucleotide phosphodiesterase activity, similar to the full peptide. This suggests the opiate-binding region is not essential for calmodulin interaction.

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    Ratiometric pulsed alkylation/mass spectrometry of the cysteine pairs in individual zinc fingers of MRE-binding transcription factor-1 (MTF-1) as a probe of zinc chelate stability.

    Biochemistry·2001

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Neuroscience

    Background:

    • Neuropeptide beta-endorphin (31 residues) inhibits calcium-dependent, calmodulin-mediated cyclic nucleotide phosphodiesterase (PDE) activity.
    • The N-terminal region of beta-endorphin is known to mediate opiate receptor interactions.

    Purpose of the Study:

    • To investigate the role of the N-terminal region of beta-endorphin in calmodulin interaction.
    • To determine if a synthetic N-terminal deletion peptide retains inhibitory activity against calmodulin-stimulated PDE.

    Main Methods:

    • Enzyme activity assays measuring cyclic nucleotide phosphodiesterase inhibition.
    • Circular dichroic spectroscopy to assess peptide-protein interactions and conformational changes.

    Main Results:

    • A synthetic N-terminal deletion peptide (des-(1-13)) of beta-endorphin inhibited stimulated PDE activity with the same efficacy as intact beta-endorphin.
    • The des-(1-13) peptide did not affect basal PDE activity.
    • Circular dichroic spectroscopy indicated enhanced alpha-helicity in the des-(1-13) beta-endorphin upon binding to calmodulin, suggesting helix formation.

    Conclusions:

    • The N-terminal region of beta-endorphin, responsible for opiate activity, is not required for calmodulin interaction.
    • The C-terminal portion of beta-endorphin mediates the inhibition of calmodulin-stimulated PDE activity.
    • The interaction involves an increase in alpha-helicity of the peptide, potentially forming an amphipathic helix.

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