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UID:69dc782eaa665
DTSTAMP:20260413T005926
DTSTART:20160923T110000
SEQUENCE:0
TRANSP:OPAQUE
DTEND:20160923T123000
URL:https://murmitoyen.com/events/vanille/udem/detail/716407-seminaire-de-l
 etudiante-azade-geranurimi-groupe-lubell
LOCATION:Université de Montréal - Pavillon J.-Armand-Bombardier\, 5155\, 
 chemin de la rampe \, Montréal\, QC\, Canada\, H3T 2B2
SUMMARY:Séminaire de l'étudiante Azade Geranurimi (Groupe Lubell)
DESCRIPTION:Titre : Synthesis of β-substituted-α-amino γ-lactams to stud
 y the influence of peptide-based conformational constraint on IL-1 alloste
 ric modulatorsEndroit : Pavillon J.-Armand Bombardier\, salle 1035 à 11
  h 00.
\nCette conférence sera prononcée par Madame Azade Geranurimi\, 
 étudiante au doctorat\, du laboratoire de William Lubell\, professeur au
  Département de chimie de l'Université de Montréal.
\nRésumé:
\nPepti
 de 101.10 (rytvela) is an allosteric modulator of the interleukin 1 recept
 or\, which has potential clinical applications in inflammation. The threon
 ine residue of this peptide may play an important role in activity and rec
 eptor recognition through hydrogen bonding by way of the side chain hydrox
 y group. Towards the design of constrained threonine analogs to explore th
 e impact of conformation on peptide biology\, we have targeted the synthes
 is of α-amino-β-hydroxy-γ-lactam (Hgl) analogs of 101.10 (rytvela). By 
 restricting rotation about the ω\, ψ\, and χ dihedral angles\, the Hgl 
 residue is expected to stabilize a potential β-turn structure that may be
  responsible for potency and selectivity. Eight different isomers of the H
 gl-Val dipeptide were synthesized for insertion into the sequence of 101.1
 0 (rytvela) by solid phase synthesis to investigate the influence of confi
 guration on conformation and biological activity. In addition\, four isome
 rs of α-amino-γ-lactam (Agl)-Val dipeptides have been synthesized and in
 corporated into the sequence of 101.10 (rytvela) as controls to explore th
 e effect of hydroxyl group in biological activity. All of Agl and Hgl dias
 teriomers of 101.10 have been biologically tested. Preliminary biological 
 studies were promising and resulted in further investigation to understand
  the nature of hydroxyl group interaction with the receptor and possible e
 ffects on conformation by functionalizing it to series of groups such as S
 H\, NH2\, F\, CO2H\, CONH2 and triazole. So far thiol and amine substitute
 d α-amino-γ-lactam have been synthesized and the rest are in perspective
 .
\nInformation supplémentaireAnnonce PDF du séminaire
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