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SUMMARY:Probing the Conformation of Gas Phase Biomolecular Ions by Forster
  Resonance Energy Transfer and Ion Mobility Mass Spectrometry
DTSTART:20151112T163000
DTEND:20151112T173000
DTSTAMP:20260916T043943Z
UID:b78492792c3ae17360884d76344856cb55a440308021ec96ab0f8069
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Philippe Dugourd\nInstitut Lumière Matière\nCNRS & Uni
 versité Lyon 1\, France\nStructural measurement in the gas phase is fuele
 d by developments in the mass spectrometry community to carry out “nativ
 e” electrospray ionization to obtain gas-phase biomolecular ions with a 
 conformation that is presumably close to the native one. In Lyon\, we try 
 to push Mass Spectrometry and Optics beyond traditional areas to understan
 d the structure and aggregation of proteins.\nFörster resonant energy tra
 nsfer (FRET) is a strongly distance sensitive optical method and can be us
 ed as a “spectroscopic ruler” to obtain distance constraints within a 
 molecule. The transposition of this technique to the gas phase is appealin
 g since it opens the perspective of combining the structural accuracy of F
 RET with the specificity and selectivity of mass spectrometry. During this
  talk\, we will present a methodology for measuring FRET in the gas-phase 
 based on the detection of specific photo-fragmentation rather than fluores
 cence. The structural sensitivity of the method was tested using chromopho
 res grafted on a series of small alanine based peptides.1\nSmall oligomers
  of the amyloid beta protein have been implicated as the neurotoxic agent 
 leading to Alzheimer's disease\, and in particular mutations in the hydrop
 hobic core region comprising amino acids L17 to A21 have a large influence
  on the propensity for aggregate formation. In order to understand the ori
 gin of this behavior\, the gas phase conformations for the different charg
 e states of the wild-type 12–28 fragment of the amyloid beta and its F19
 P alloform were studied by a combination of action-FRET\, ion-mobility spe
 ctrometry (IMS) and molecular dynamics simulations.2 Ongoing experiments o
 n proteins will also be discussed. \nFinally\, we have just achieved the 
 construction of a new experimental set-up which couples tandem-IMS with la
 ser excitation.3 This set-up allows to record optical spectra on isomer se
 lected biomolecular ions. The Influence of charge localization on the conf
 ormation and on the optical spectrum of a small peptide will be presented.
 \n1 S. Daly\, F. Poussigue\, A.-L. Simon\, L. MacAleese\, F. Bertorelle\, 
 F. Chirot\, R. Antoine and P. Dugourd. Anal. Chem. 86\, 8798–8804 (2014)
 .\n2 S. Daly\, A. Kulesza\, F. Poussigue\, A.-L. Simon\, C.-M. Choi\, G. K
 night\, F. Chirot\, L. MacAleese\, R. Antoine and P. Dugourd. Chem. Sci. 6
 \, 5040 –5047 (2015).\n3 A.-L. Simon\, F. Chirot\, C.-M. Choi\, C. Clavi
 er\, M. Barbaire\, J. Maurelli\, X. Dagany\, L. MacAleese and P. Dugourd. 
 Rev. Sci. Instrum. 86\, 094101 (2015).
LOCATION:CH G1 495 https://plan.epfl.ch/?room==CH%20G1%20495
STATUS:CONFIRMED
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