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SUMMARY:From protein total synthesis to peptide transamidation and metathe
 sis: Playing with the reversibility of N\,S- or N\,Se-acyl migration react
 ions
DTSTART:20140917T171500
DTEND:20140917T181500
DTSTAMP:20260919T215530Z
UID:61b464f7faeca8141ef7b3c98ef9bc854328bf649a0bc5c274d7e56b
CATEGORIES:Conferences - Seminars
DESCRIPTION:Prof. Oleg Melnyk\, Institut Pasteur of Lille\, France\nChemos
 elective amide bond forming reactions which proceed efficiently in water a
 t neutral pH enable the sequential assembly of peptide segments and thus t
 he total synthesis of large peptides or proteins.1 These reactions are als
 o useful tools for accessing to complex peptide scaffolds such as branched
  or cyclic peptides. The native chemical ligation (NCL) reaction is centra
 l to the field of protein total synthesis\, but other amide bond forming r
 eactions are emerging\, which in combination with NCL can facilitate the a
 ccess to large peptides or peptidic scaffolds. In particular\, the bis(2-s
 ulfanylethyl)amido (SEA) N\,S-acyl shift system enabled the development of
  an array of useful chemical tools for peptide ligation2 or peptide thioes
 ter3-7 and thioacid8 synthesis. SEA chemistry permitted also the developme
 nt of N-to-C sequential peptide segment assembly methods for protein synth
 esis in solution3\,9\,10 or on a solid-phase.11 The lecture will present t
 he main features of SEA chemistry as well as the potential of SEA and SeEA
 \, i.e. the selenium analog of SEA group\, for the synthesis of functional
  proteins derived from the hepatocyte growth factor (HGF) or peptide scaff
 olds. It will discuss also the potential of N\,Se-acyl shift systems for d
 esigning native peptide metathesis reactions.12
LOCATION:BCH 2218 https://plan.epfl.ch/?room==BCH%202218
STATUS:CONFIRMED
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