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Sequential and Environmental Dependence of Conformation in a Small Opioid Peptide

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    Sequential and Environmental Dependence of Conformation in a Small Opioid Peptide
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    • Alexandra C. Schwartz
      Alexandra C. Schwartz
      Department of Chemistry and Biochemistry, College of Charleston, Charleston, South Carolina 29424, United States
      More by Alexandra C. Schwartz
    • Dashiell W. Jay
      Dashiell W. Jay
      Department of Chemistry and Biochemistry, College of Charleston, Charleston, South Carolina 29424, United States
      More by Dashiell W. Jay
    • Stuart Parnham
      Stuart Parnham
      Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, South Carolina 29425, United States
      More by Stuart Parnham
    • Michael W. Giuliano*
      Michael W. Giuliano
      Department of Chemistry and Biochemistry, College of Charleston, Charleston, South Carolina 29424, United States
      *E-mail: [email protected]
      More by Michael W. Giuliano
      Orcidhttp://orcid.org/0000-0003-0137-7769
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    The Journal of Organic Chemistry

    Cite this: J. Org. Chem. 2019, 84, 21, 13299–13312
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    https://doi.org/10.1021/acs.joc.9b01141
    Published September 20, 2019
    Copyright © 2019 American Chemical Society
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    Abstract

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    We report the structural characterization of the μ-selective endogenous opioid endomorphin-1 (EM-1) via an array of nuclear magnetic resonance experiments in both aqueous conditions and, for the first time, in isotropic lipid bicelles, which mimic its endogenous environment. Consistent with computationally derived hypotheses, EM-1 is found to significantly populate a compact, turn-like structure in aqueous solution. This structure is only present as a minor species when the peptide is subjected to a lipid environment, in which the presented NMR data suggests that the major conformer of EM-1 lacks internal hydrogen bonds. The interaction of EM-1 with lipid bilayers is characterized by both tryptophan fluorescence and two-dimensional diffusion ordered NMR spectroscopy; these experiments suggest that the interaction with the surface of phospholipid bilayers, operating as a change in bulk solvation, is responsible for the observed conformational rearrangement in EM-1.

    Copyright © 2019 American Chemical Society

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    Supporting Information

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    The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acs.joc.9b01141.

    • Depictions of MD trajectories for the 1 and 2 (full.dcd/coordinate files are available upon request); initial coordinate and parameter files along with NAMD scripts used to generate the trajectories; all NMR spectra; MALDI-time-of-flight (TOF) mass spectra; chemical shift assignment tables and tables of distance restraints for all 2D datasets and ensembles; coordinate files for all final NMR structure ensembles; and fluorescence spectra (PDF)

    • All chemical shift data for endomorphin-1 (peptide 1) in this study has been deposited in the Biological Magnetic Resonance Bank under accession number 27756. Coordinates are provided for all NMR ensembles as additional Supporting information: pept1_aq_ensemble (si_002.pdb)

    • pept1_minor_lipids_ensemble (si_003.pdb)

    • pept1_major_lipids_ensemble (si_004.pdb)

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    Most electronic Supporting Information files are available without a subscription to ACS Web Editions. Such files may be downloaded by article for research use (if there is a public use license linked to the relevant article, that license may permit other uses). Permission may be obtained from ACS for other uses through requests via the RightsLink permission system: http://pubs.acs.org/page/copyright/permissions.html.

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    This article is cited by 3 publications.

    1. Katelyn N. Kraichely, Sarah E. Clinkscales, Cecilia M. Hendy, Eric A. Mendoza, Stuart Parnham, Michael W. Giuliano. Minimal Increments of Hydrophobic Collapse within the N-Terminus of the Neuropeptide Galanin. Biochemistry 2022, 61 (12) , 1151-1166. https://doi.org/10.1021/acs.biochem.2c00141
    2. Erin C. Day, Keila C. Cunha, Roy J. Zhao, Audra J. DeStefano, James N. Dodds, Melissa A. Yu, Jaina R. Bemis, Songi Han, Erin S. Baker, Joan-Emma Shea, Rebecca B. Berlow, Abigail S. Knight. Insights into conformational ensembles of compositionally identical disordered peptidomimetics. Polymer Chemistry 2024, 15 (29) , 2970-2980. https://doi.org/10.1039/D4PY00341A
    3. Rachel E. Wilkinson, Katelyn N. Kraichely, Cecilia M. Hendy, Lauren E. Buchanan, Stuart Parnham, Michael W. Giuliano. The neuropeptide galanin adopts an irregular secondary structure. Biochemical and Biophysical Research Communications 2022, 626 , 121-128. https://doi.org/10.1016/j.bbrc.2022.08.032
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    The Journal of Organic Chemistry

    Cite this: J. Org. Chem. 2019, 84, 21, 13299–13312
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acs.joc.9b01141
    Published September 20, 2019
    Copyright © 2019 American Chemical Society
    Request reuse permissions

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