title: Resonance Energy Transfer Relates the Gas-Phase Structure and Pharmacological Activity of Opioid Peptides.
abstract: Enkephalins are efficient pain-relief drugs that bind to transmembrane opioid receptors. One key structural parameter 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 spectrometry, 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.
authors.affiliation: Laboratoire de Chimie Physique Moléculaire, École Polytechnique Fédérale de Lausanne, 1015 Lausanne (Switzerland).
authors.forename: Vladimir
authors.initials: V
authors.lastname: Kopysov
authors.affiliation: Laboratoire de Chimie Physique Moléculaire, École Polytechnique Fédérale de Lausanne, 1015 Lausanne (Switzerland). oleg.boiarkin@epfl.ch.
authors.forename: Oleg V
authors.initials: OV
authors.lastname: Boyarkin
mesh_terms: D004735:Energy Transfer; D005740:Gases; D018847:Opioid Peptides / Q000494:pharmacology*; D013057:Spectrum Analysis
chemical_list: D005740:Gases; D018847:Opioid Peptides
keywords: FRET; enkephalins; mass spectrometry; peptides; photodissociation