BEGIN:VCALENDAR
VERSION:2.0
PRODID:-//Memento EPFL//
BEGIN:VEVENT
SUMMARY:Synthesis of biologically active compounds. From chiral amines to 
 protein degraders
DTSTART:20250430T171500
DTEND:20250430T180000
DTSTAMP:20260917T052627Z
UID:715ba59ab86c0e815147c113cce4840db3b6820662f458c2983844dc
CATEGORIES:Conferences - Seminars
DESCRIPTION:Dr.Antoni Riera Escalé\nInstitut de Recerca Biomèdica (IRB B
 arcelona) Departament de Química Orgànica\nUniversitat de Barcelona\n \
 n\n\nAbstract. The development of a new drug is a very complex and difficu
 lt process. It starts with the identification of a biological target (very
  often a protein) whose biological activity needs to be modified. In most 
 occasions\, the way to modify its action is based on the inhibition of its
  enzymatic activity by a small molecule. To find a good inhibitor is a dif
 ficult task but\, once achieved\, it is necessary to develop an efficient 
 and environmentally benign synthetic procedure. On the other hand\, many d
 rugs are chiral and need to be prepared in high enantiomeric purity. Asymm
 etric hydrogenation is perhaps one of the best methodologies for the large
 -scale preparation of chiral drugs [1]. We will discuss some of the develo
 pments done by our group on the asymmetric hydrogenation of chiral amines\
 , key components of many drugs [2].\nIn recent years a new pharmacological
  approach has been developed that might potentially overcome the shortcomi
 ngs of traditional inhibitors: targeted protein degradation. PROTACs (prot
 eolysis targeting chimeras) are heterobifunctional molecules that hijack t
 he ubiquitin-proteasome system (UPS)\, native to eukaryotic cells\, to ind
 uce degradation of a protein of interest (POI) [3]. We will describe the d
 esign\, synthesis\, and optimization of degraders targeting two important 
 proteins: the p38 MAP Kinase [4] and the oestrogen receptor [5].\n\n© 202
 5 EPFL\n\nFigure 1. Representative chiral small-molecule drugs and an oest
 rogen receptor protac.\n\nReferences:\n[1] A. Cabre\, X. Verdaguer\, A. Ri
 era\, Chem. Rev. 122\, 269-339 (2022).\n[2] a) E. Salomo\, S. Orgue\, A. R
 iera\, X. Verdaguer\, Angew. Chem.\, Int. Ed. 55\, 7988-7992 (2016). b) P.
  Rojo\, M. Molinari\, A. Cabre\, C. Garcia-Mateos\, A. Riera\, X. Verdague
 r\, Angew. Chem.\, Int. Ed. 61\, e202204300 (2022). c) Y. Wen\, M. Fernán
 dez-Sabaté\, A. Lledós\, G. Sciortino\, J. Eills\, I. Marco-Rius\, A. Ri
 era\, X. Verdaguer\, Angew Chem Int Ed Engl\, e202404955 (2024).\n[3] Li\,
  K.\; Crews\, C. M. Chem. Soc. Rev.\, 51\, 5214-5236 (2022).\n[4] C. Donog
 hue\, M. Cubillos-Rojas\, N. Gutierrez-Prat\, C. Sanchez-Zarzalejo\, X. Ve
 rdaguer\, A. Riera\, A. R. Nebreda\, Eur. J. Med. Chem. 2020\, 201\, 11245
 1.\n[5] G. Loren\, I. Espuny\, A. Llorente\, C. Donoghue\, X. Verdaguer\, 
 R. R. Gomis\, A. Riera\, Eur. J. Med. Chem. 243\, 114770 (2022).\n\n\n\n 
LOCATION:Salle Unil Genopode A
STATUS:CONFIRMED
END:VEVENT
END:VCALENDAR