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SUMMARY:Chemical Biology of Uniquely Modified Peptides and Proteins
DTSTART:20220822T161500
DTEND:20220822T173000
DTSTAMP:20260916T225612Z
UID:c1a8baa108d50a575fb889404336d902028097d7e63113054c123020
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Ashraf Brik (Technion Israel Institute of Technology)\nC
 hemical Protein synthesis offers great opportunities to synthesize uniquel
 y modified proteins (e.g.\, ubiquitinated proteins) with high homogeneity 
 and workable quantities. The field relies on the synthesis of peptide frag
 ments and the ligation of these peptides in their unprotected forms employ
 ing different ligation strategies. We have recently reported that transiti
 on metals such as palladium and gold complexes can be used remove multiple
  Cys protecting groups within minutes in a fully aqueous medium\, which co
 uld be coupled in-situ with native chemical ligation to provide excellent 
 yields of the desired product. We have also demonstrated unprecedented gol
 d mediated depropargylation from an amide bond to facilitate the synthesis
  of difficult peptides and proteins. This chemistry was further developed 
 for the cyclization of a wide range of peptides that modulate the function
  of ubiquitin chains. Furthermore\, we extend our chemistry for the remova
 l of protecting groups from Cys residues for the rapid and one-pot disulfi
 de bond formation in various bioactive peptides. Finally\, using this chem
 istry we developed a strategy for the cellular delivery and on demand acti
 vation of synthetic proteins.
LOCATION:BCH 2218 https://plan.epfl.ch/?room==BCH%202218
STATUS:CONFIRMED
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