Resonance Energy Transfer Relates the Gas-Phase Structure and Pharmacological Activity of Opioid Peptides

Enkephalins are efficient pain-relief drugs that bind to transmembrane opioid receptors. One key structural param- eter that governs the pharmacological activity of these opioid peptides and is typically determined from condensed-phase structures is the distance between the aromatic rings of their Tyr and Phe residues. We use resonance energy transfer, detected by a combination of cold ion spectroscopy and mass spec- trometry, to estimate the Tyr–Phe spacing for enkephalins in the gas phase. In contrast to the condensed-phase structures, these distances appear to differ substantially in enkephalins with different pharmacological efficiencies, suggesting that gas- phase structures might be a better pharmacophoric metric for ligand peptides.


Published in:
Angewandte Chemie -International Edition in English-, 55, 2, 689-692
Year:
2016
Publisher:
Wiley-Blackwell
ISSN:
1433-7851
Keywords:
Laboratories:


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 Record created 2015-11-17, last modified 2018-03-17

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