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SUMMARY:Macrocyclic peptide inhibitors of protein-RNA interactions
DTSTART:20240423T101500
DTEND:20240423T111500
DTSTAMP:20260916T032120Z
UID:6676e4276e9c4fc8a2d453cb6adf985513cea4a9b4d8515ded256167
CATEGORIES:Conferences - Seminars
DESCRIPTION:Dr. Peter t'Hart\, Group Leader Chemical Genomics Centre\, Max
  Planck Institute for Molecular Physiology\, Dortmund\nProtein-RNA interac
 tions are essential in the regulation and function of any given RNA. Aberr
 ant formation of such interactions can therefore rapidly lead to disease m
 aking them attractive therapeutic targets. Targeting such interactions is 
 challenging however since they involve large interfaces and typically lack
  well defined pockets. To overcome this challenge\, we take inspiration f
 rom strategies originally developed to identify protein-protein interactio
 n inhibitors and adapt them for protein-RNA interaction inhibitors. The fi
 rst strategy we used is structure-based design of stapled peptides as inhi
 bitors of the splicing factor polypyrimidine-tract binding protein 1 (PTBP
 1). By exploring various stapling strategies\, an inhibitory peptide was 
 identified that was stable against proteolysis as well as cell permeable a
 nd able to modulate splicing events regulated by PTBP1. When a given targe
 t lacks structural information a structure-based design approach can’t b
 e used. To be able to identify inhibitors in this situation we use genetic
 ally encoded cyclic peptide libraries (i.e.: SICLOPPS) in combination with
  an in-house developed assay to screen for inhibitory peptides of the spli
 cing factor hnRNP A2/B1. Preliminary data shows that hits can be found fr
 om a single screening round when combined with next generation sequencing 
 and that structural optimization is feasible.
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STATUS:CONFIRMED
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