title: IRMPD Spectroscopy: Evidence of Hydrogen Bonding in the Gas Phase Conformations of Lasso Peptides and their Branched-Cyclic Topoisomers.
abstract: Lasso peptides are natural products characterized by a mechanically interlocked topology. The conformation of lasso peptides has been probed in the gas phase using ion mobility-mass spectrometry (IM-MS) which showed differences in the lasso and their unthreaded branched-cyclic topoisomers depending on the ion charge states. To further characterize the evolution of gas phase conformations as a function of the charge state and to assess associated changes in the hydrogen bond network, infrared multiple photon dissociation (IRMPD) action spectroscopy was carried out on two representative lasso peptides, microcin J25 (MccJ25) and capistruin, and their branched-cyclic topoisomers. For the branched-cyclic topoisomers, spectroscopic evidence of a disruption of neutral hydrogen bonds were found when comparing the 3+ and 4+ charge states. In contrast, for the lasso peptides, the IRMPD spectra were found to be similar for the two charge states, suggesting very little difference in gas phase conformations upon addition of a proton. The IRMPD data were thus found consistent and complementary to IM-MS, confirming the stable and compact structure of lasso peptides in the gas phase.
authors.affiliation: Normandie Univ, COBRA, UMR 6014, FR 3038; Univ Rouen; INSA Rouen; CNRS , 1 Rue Tesnière, 76821 Mont-Saint-Aignan Cedex, France.
authors.forename: Kevin
authors.initials: K
authors.lastname: Jeanne Dit Fouque
authors.affiliation: Normandie Univ, COBRA, UMR 6014, FR 3038; Univ Rouen; INSA Rouen; CNRS , 1 Rue Tesnière, 76821 Mont-Saint-Aignan Cedex, France.
authors.forename: Hélène
authors.initials: H
authors.lastname: Lavanant
authors.affiliation: Muséum national d'Histoire naturelle, Sorbonne Universités, Centre national de la Recherche scientifique, Laboratoire Molécules de Communication et Adaptation des Microorganismes, UMR 7245 CNRS-MNHN, CP 54 , 57 rue Cuvier, 75005 Paris, France.
authors.forename: Séverine
authors.initials: S
authors.lastname: Zirah
authors.affiliation: Laboratoire de Chimie Physique, Université Paris Sud, UMR 8000 CNRS, Faculté des Sciences, Bât. 349 , 91405 Orsay Cedex, France.
authors.forename: Vincent
authors.initials: V
authors.lastname: Steinmetz
authors.affiliation: Muséum national d'Histoire naturelle, Sorbonne Universités, Centre national de la Recherche scientifique, Laboratoire Molécules de Communication et Adaptation des Microorganismes, UMR 7245 CNRS-MNHN, CP 54 , 57 rue Cuvier, 75005 Paris, France.
authors.forename: Sylvie
authors.initials: S
authors.lastname: Rebuffat
authors.affiliation: Laboratoire de Chimie Physique, Université Paris Sud, UMR 8000 CNRS, Faculté des Sciences, Bât. 349 , 91405 Orsay Cedex, France.
authors.forename: Philippe
authors.initials: P
authors.lastname: Maître
authors.affiliation: Normandie Univ, COBRA, UMR 6014, FR 3038; Univ Rouen; INSA Rouen; CNRS , 1 Rue Tesnière, 76821 Mont-Saint-Aignan Cedex, France.
authors.forename: Carlos
authors.initials: C
authors.lastname: Afonso
mesh_terms: D000595:Amino Acid Sequence; D001430:Bacteriocins / Q000737:chemistry*; D005740:Gases / Q000737:chemistry*; D006860:Hydrogen Bonding; D007536:Isomerism; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared
chemical_list: D001430:Bacteriocins; D005740:Gases; D010455:Peptides; C533129:capistruin; C020411:microcin