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DTSTAMP:20260411T190841
DTSTART:20180221T110000
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URL:https://murmitoyen.com/events/vanille/udem/detail/798935-a-peptide-orth
 otic-toolkit-for-protein-mimicry
LOCATION:Université de Montréal - Pavillon J.-Armand-Bombardier\, 5155\, 
 chemin de la rampe \, Montréal\, QC\, Canada\, H3T 2B2
SUMMARY:A Peptide Orthotic Toolkit for Protein Mimicry
DESCRIPTION:Cette conférence sera prononcée par le Professeur Juan Del
  Valle du département de chimie de la University of South Florida.
\nHô
 te : William Lubell
\nRésumé :Interactions between peptide secondary str
 uctures mediate a broad array of biological processes and provide design c
 ues for the discovery of new chemical probes\, therapeutics\, and biomater
 ials. Despite the critical role of a-helices\, b-sheets\, and polyproline 
 helices in human physiology\, the development of molecules capable of modu
 lating their interactions remains a significant challenge. Our laboratory 
 has a long-standing interest in the design of protein domain mimics that a
 ddress the bioavailability\, stability\, and functional limitations of nat
 ive peptide sequences. At the center of our research program is the develo
 pment of efficient synthetic methods that will enable the construction of 
 “made-to-order” proteomimetics using readily accessible building block
 s. Toward this end\, we have described novel classes of peptide orthotics 
 that nucleate b-sheet folds through backbone N-amino and N-hydroxy substit
 ution. In addition to covalent tethering sites\, these substituents provid
 e key steric\, electrostatic\, and hydrogen bonding interactions that serv
 e to stabilize and mimic protein secondary structure. Cyclic derivatives o
 f N-amino peptides are also used to constrain a-helix\, b-turn and polypro
 line II motifs through non-covalent interactions. Our secondary structure 
 mimics have recently been employed in the design of oncogenic protein-prot
 ein interaction inhibitors\, modulators of neurodegenerative amyloid aggre
 gation\, and unnatural mimics of collagen triple helices. These efforts br
 ing us one step closer to a ‘universal’ approach toward protein mimicr
 y with broad-ranging applications in chemical biology and molecular recogn
 ition.
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\nInformations supplémentaires
\nAnnonce PDF de la conférence

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