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PRODID:https://murmitoyen.com/events/vanille/udem/
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UID:69e1a2ed6eb21
DTSTAMP:20260416T230309
DTSTART:20121212T113000
SEQUENCE:0
TRANSP:OPAQUE
DTEND:20121212T130000
URL:https://murmitoyen.com/events/vanille/udem/detail/155102
LOCATION:Université de Montréal - Pavillon J.-Armand-Bombardier\, 5155\, 
 chemin de la rampe \, Montréal\, QC\, Canada\, H3T 2B2
SUMMARY:Conférence de la Professeure Anna Maria Papini (Florence)
DESCRIPTION:Titre : A 'Chemical Reverse Approach' to Modulate Peptide Secon
 dary StructuresInducing Specific and High Affinity Biological Recognition.
 Cette conférence sera prononcée par la professeure Anna Maria Papini du 
 Laboratoire français-italien de chimie des peptides et protéine et de sy
 nthèse organique sélective et chimie bioorganique (PeptLab-SOSCO)\, affi
 lié à l'Université de Florence et à l'Université de Cergy Pontoise. C
 ette dernière sera à Montréal à titre d'examinatrice externe d'une sou
 tenance de thèse en chimie. Elle sera prononcée en anglais.Résumé : Pe
 ptides are interesting tools to be used as model systems when they are abl
 e to reproduce biologically relevant small protein structures. However pep
 tides\, especially short ones (constrain inside a peptide sequence in orde
 r to lock a given conformation\, i.e.\, β-turn and α-helix\, possibly re
 producing the bioactive conformation. In this context\, we defined 'Chemic
 al Reverse Approach' the strategy followed to stabilise peptide conformati
 ons inducing specific and high affinity biological recognition. In the las
 t years we performed as a proof-of-concept a systematic work demonstrating
  that 1\,4-disubstituted [1\,2\,3]triazolyl moiety (bioisosteric to the pe
 ptide bond) introduced as a replacement of i-to-i+4 side chain-to-side cha
 in bridging lactam in peptides derived from parathyroid hormone-related pr
 otein (PTHrP)\, was able to reproduce the bioactive α-helical structure. 
 Thus\, we applied the [1\,2\,3]triazolyl-bridging strategy to stabilize a 
 β-turn conformation in MTII. In particular we replaced the lactam bridge 
 with a i-to-i+5 side chain-to-side chain cyclization via CuI-catalyzed azi
 do-to-alkyne 1\,3-dipolar cycloaddition (CuAAC) generating 1\,4- disubstit
 uted [1\,2\,3]triazolyl-containing ring structures. The clicked MTII analo
 gs presenting different permutations of bridges with different methylene n
 umbers and a triazolyl moiety were synthesized by a combination of solid p
 hase assembly of the peptide and in solution CuAAC. The biological activit
 y (EC50) towards the principal murine melanocortin receptors of several li
 near and cyclic MTII peptide analogs compared to the NMR conformational st
 udies lead to an interesting correlation. Such 'Chemical Reverse Approach
 ' was amazingly useful to develop efficient diagnostic/prognostic assays f
 or autoimmune diseases. In fact\, β-turn peptide structures and multivale
 nt structures (MEPs) optimally exposing multiple copies of possible aberra
 nt post-translationally modified minimal epitopes (mimicking bacterial and
 /or viral infections\, xenobiotics\, etc.) were able to increase recogniti
 on affinity\, making possible to detect and fishing out specific autoantib
 odies present in sera of patients affected by neurodegenerative/neurodevel
 opment immune mediated diseases\, i.e. multiple sclerosis and autistic per
 vasive disorders (Rett Syndrome). Interestingly\, the autoantibodies purif
 ied by peptide-based immunoaffinity columns were able to select possible c
 andidate protein autoantigens involved in neurodegeneration. Therefore\, s
 pecific peptide-based apheresis could be a challenging non invasive immuno
 therapeutic strategy for children neurodegenerative diseases. Information 
 supplémentaire au sujet d'Anna Maria PapiniInterdepartmental Laboratory o
 f Peptide and Protein Chemistry and Biology (PetLab)
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