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DTSTART:20171107T110000
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URL:https://murmitoyen.com/events/vanille/udem/detail/788455-new-perspectiv
 es-for-proteomics-biomedical-and-biomolecular-epitope
LOCATION:Pavillon Roger-Gaudry \, 2900\, boul. Édouard-Montpetit\, Local M
 -415\, Montréal\, QC\, Canada
SUMMARY:New Perspectives for Proteomics\, Biomedical and Biomolecular Epito
 pe
DESCRIPTION:Conférence de chimie
\nTitre completNew Perspectives for Prote
 omics\, Biomedical and Biomolecular Epitope\, Determination by Combination
  of Affinity Tools and Mass Spectrometry
\nCette conférence sera prononc
 ée (en anglais) par le Professeur Michael Przybylski du Steinbeis Cente
 r for Biopolymer Analysis and Biomedical Mass Spectrometry\, University of
  Konstanz.
\nHôte : Joelle Pelletier
\nRésumé: Bioaffinity-based techno
 logies such as ELISA\, Western Blot and biosensor determination are long e
 stablished in the analysis of biomolecular interactions\, but their combin
 ation with mass spectrometry (MS) is only beginning to be explored. Bioaff
 inity and MS technologies are recently emerging as powerful “hybrid” t
 ools for detection\, chemical structure determination and quantification o
 f biomolecular interactions\, particularly recognition epitopes. New devel
 opments of MS for the characterization of biopolymer interactions will be 
 reviewed by combination with biochemical affinity techniques\; affinity-se
 paration\, affinity determination and quantification\; identification of a
 ntigen epitopes and antibody paratopes\; clinical applications of affinity
 - protomics. These technologies are currently gaining high interest in man
 y application areas such as pharmacology\, clinical diagnostics and the de
 velopment of antibody-based drugs.
\nBioaffinity analysis using biosensors
  such as surface plasmon resonance (SPR) has become an established techniq
 ue for the detection and quantification of biomolecular interactions. Howe
 ver\, a principal limitation of biosensors is their lack of providing chem
 ical structure information of affinity-bound ligands. Proteolytic excision
 /extraction (Protex-MS)\, hydrogen-deuterium exchange (HDX-MS) of peptide 
 backbone hydrogens\, and Fast- Photochemical Oxidation (FPOP) are major te
 chniques for mass spectrometry based elucidation of protein- ligand intera
 ctions\, but none of these tools alone provide quantitative affinity data.
 
\nWe have developed an online SPR- biosensor-MS combination with electros
 pray ionization mass spectrometry that enables the simultaneous affinity i
 solation\, chemical structure determination and affinity quantification of
  protein and peptide epitopes [Patent pending\; 2016]. Key tool of the SPR
 - MS combination is an integrated\, automated interface that provides samp
 le concentration and in-situ desalting for MS analysis of the ligand eluat
 e [1]. ESI-MS instruments from all major manufacturers and a wide range of
  biosensors (in addition to SPR) can be coupled. Recent applications of th
 e online SPR- MS show broad bioanalytical potential and high performance f
 or interaction studies and epitope characterization from biological materi
 al\, as diverse as antigen-antibody and lectin- carbohydrate complexes\; a
 ffinity binding constants (KD) determinations are well feasible from milli
 - to nanomolar ranges [2\, 3]. First applications to the direct analysis o
 f biological samples\, such as cell lysate and tissue homogenate will be d
 iscussed.
\n
\nSlamnoiu\, S. et al. (2014) J.Am. Soc. Mass Spectrom. 25\, 
 1472-1481.
\nPetre\, A\, et al. (2012) J. Am. Soc. Mass Spectrom.\, 23\, 1
 831-11840. [3] 
\nMoise\, A.\, et al.\, (2011) J. Am. Chem. Soc. 133\, 148
 44-14847.
\nVlad\, C. et al.\, (2011) ChemBiochem. 12\, 2740-2744.
\nPrzyb
 ylski\, M. et al.\, (2016) Anal. Bioanal. Chem. In press.
\n
\nInformation
 s supplémentairesAnnonce PDF de la conférence
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