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UID:69e152d4e4abc
DTSTAMP:20260416T172124
DTSTART:20130315T140000
SEQUENCE:0
TRANSP:OPAQUE
DTEND:20130315T153000
URL:https://murmitoyen.com/events/vanille/udem/detail/153928
LOCATION:Université de Montréal - Pavillon Roger-Gaudry\, 2900\, chemin d
 e la Tour\, Montréal\, QC\, Canada\, H3T 1J6
SUMMARY:Conférence de la Professeure Cornelia Bohne (Victoria)
DESCRIPTION:Titre :  Supramolecular Dynamics and Function for Host-Guest S
 ystems with Increasing Complexity: From Cucurbit[n]urils to Bile Salt Aggr
 egates and  Serum Albumins.La conférence sera prononcée par la professe
 ure Cornelia Bohne du Département de chimie de l'University of Victoria. 
 Elle sera donnée en anglais. Résumé : Supramolecular systems are alway
 s reversible and characterization of their dynamics is essential to unders
 tand and control their function. The kinetics for the association and diss
 ociation processes of the building blocks of interest are measured using f
 ast kinetic techniques. The characterization of the dynamics of guest bind
 ing with cucurbit[n]urils (CB[n]) showed that the exceptionally high equil
 ibrium constants for guest binding are achieved because the dissociation p
 rocesses are much slower than observed for other macrocycles. The presence
  of cations\, which can bind to the portals of CB[n]s\, and the structure 
 of the guest influence the type of mechanism observed for the guest-CB[n] 
 dynamics. Bile salt aggregates are host systems with increased complexity 
 because of the presence of binding sites with different properties. Bile s
 alt aggregates in solution and as gels are excellent hosts to solubilize w
 ater insoluble functional guests\, such as photochromic compounds. Multipl
 e colors were achieved for photochromic compounds incorporated into bile s
 alt gels eliminating the need for the synthesis of molecules with tethered
  chromophores. Serum albumins are chiral host systems that were employed t
 o enhance the chiral discrimination of a bimolecular model reaction. Photo
 physical measurements showed that the highest enantiomeric excess is achie
 ved when the reagent is bound to a protein site for which exchange dynamic
 s of the reagent with the aqueous phase is fast\, but once bound the reage
 nt is immobile. Information supplémentaire
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