Sequence and Structure in Small Opioid Peptides

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dc.contributor.advisorGiuliano, Michael W
dc.contributor.authorSchwartz, Alexandra Corinne
dc.date.accessioned2022-03-29T19:01:49Z
dc.date.available2022-03-29T19:01:49Z
dc.date.created2018-05
dc.date.submittedMay 2018
dc.description.abstractMany neuropeptides lack robust structures in the protein databank, and this is sometimes attributed to assumptions regarding their flexibility. We suspect that most of these peptides do indeed have conformational preferences in aqueous solution and that these preferences likely change as the peptide approaches the membrane environment of its receptor. Additionally, we suspect that peptide structure is impacted by the addition of sidechains or residues at the C-terminus. The focus of this study are the opioid peptides: endogenous ligands of the opioid receptors, which are important drug targets for analgesics. We sought to compare the secondary structures of the endogenous opioids to that of their common N-terminal binding sequence known as the “message” sequence using computational and experimental methods. While the structural characterization of opioid peptides is ongoing, we have employed 2D 1H-1H NMR and diffusion experiments to examine the environment’s conformational influence on endomorphin-1 under both aqueous and membrane-mimetic conditions.
dc.format.mimetypeapplication/pdf
dc.identifier.urihttps://repository.library.cofc.edu/handle/123456789/5392
dc.language.isoen_US
dc.subjectneuropeptide, endomorphin-1, structure, peptide, NMR
dc.titleSequence and Structure in Small Opioid Peptides
dc.type.genrethesis
dc.type.materialtext
local.embargo.lift2019-05-01
local.embargo.terms2019-05-01
thesis.degree.departmentChemistry and Biochemistry
thesis.degree.disciplineBiochemistry
thesis.degree.grantorCollege of Charleston
thesis.degree.nameBachelor of Science
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