BEGIN:VCALENDAR VERSION:2.0 PRODID:-//Memento EPFL// BEGIN:VEVENT SUMMARY:The design of evolution and the evolution of design: Binding molec ules in biomedicine - CH635 DTSTART:20251112T161500 DTEND:20251112T171500 DTSTAMP:20260505T222607Z UID:1bf89e133767d1c46f48152130282d89238ec08a6d0ae289fde90cb3 CATEGORIES:Conferences - Seminars DESCRIPTION:Prof. Andreas Plückthun\nAbstract :\nThe lecture will highlig ht designed binding proteins and concentrate on two application areas.\n                 First\, to enable in vivo production of thera peutic proteins\, we have combined several protein engineering technologie s to devise a new platform\, termed SHielded\, REtargeted ADenovirus (SHRE AD). It is based on virus-like particles that are devoid of any viral gene s\, but contain 36 kb of DNA that can encode multiple genes and complex re gulatory regions. To target particular cells and organs\, an adapter strat egy has been devised\, based on the DARPin platform\, to selectively targe t any surface receptor of interest. To hide the particles from the immune system and to minimize liver targeting\, a protein shield was developed co vering the particles.\n                In vivo applications have included expressing therapeutic anti-tumor antibodies\, therapeutic cytokines or bispecific T-cell engagers in situ\, as well as infecting and reprogramming T-cells in vivo\, and targeting of dendritic cells in lymph nodes to co-express cytokines there for highly efficient tumor vaccinatio n.\n                Second\, we challenge the paradigm of s election from large universal libraries to obtain binding proteins rapidly and efficiently — and we also challenge the paradigm of individually de novo designing each binder for each target. When it comes to linear epito pes\, we found it possible to exploit the periodicity of peptide bonds and create a completely modular system\, based on a binding protein design th at shares the same periodicity\, using Armadillo Repeat Proteins.\n                 Using orthogonal approaches of design\, selection \, evolution\, biophysical testing\, and structure determination\, signifi cant progress has been reached toward the creation of a system of modular binding proteins that are modular and complementary to a given peptide seq uence. We believe that this technology can provide a new paradigm of creat ing binding proteins for many challenges in biomedical research.\n\nBiogra phy:\nAndreas Plückthun has been Professor of Biochemistry at the Univers ity of Zürich\, Switzerland since 1993. He studied chemistry at the Unive rsity of Heidelberg (Germany). He received a PhD from the University of Ca lifornia at San Diego in 1982 (with Ed Dennis)\, was postdoctoral fellow a t Harvard University (1982-85) (with Jeremy Knowles) and from 1985 until 1 993\, group leader at the Gene Center and Max-Planck-Institute for Biochem istry in Martinsried near Munich.\nHe has written over 500 publications\, which have been cited over 50\,000 times (h-index 130) [Google Scholar]. I n 2003\, he was elected to the German Academy of Science. In 1992\, he was elected member of EMBO.\nHe received\, among others\, the 2016 Christian- Anfinsen Award of the Protein Society for "pioneering contributions to pro tein engineering"\, and the Swiss Technology Award 2005 (Bern\, Switzerlan d) and the deVigier Award in 2005\, the JP Morgan Chase Health Award in 20 02 (San Jose\, USA) and the Wilhelm Exner Medal 2002 (Vienna\, Austria)\, the Karl-Heinz-Beckurts-Prize for 2000 (Munich\, Germany)\, and the Young Investigator's Award of the German Industry Fund.\nHe has been an inventor on more than 25 patent families and is co-founder of four companies\, Mor phosys AG (recently acquired by Novartis)\, Molecular Partners AG (Zürich \, Switzerland) and G7 Therapeutics (Zürich\, Switzerland\; merged with H eptares/Sosei [UK/Japan]) and Vector BioPharma.\nHis research in protein e ngineering has made important contributions to five areas\n\n Antibody eng ineering: he developed the first antibody expression in E. coli\, the firs t fully synthetic antibody library and made many contributions to antibody stability and design\n Scaffold engineering: he developed the repeat prot eins as alternative scaffolds\, especially the DARPin technology\, and the Armadillo technology\n Directed evolution: he developed ribosome display\ , the first truly in vitro protein evolution method\n GPCR engineering: he developed directed evolution methods for making G-protein coupled recepto rs stable for structural biology\, drug design and screening.\n Targeted g ene delivery: he developed a system of virus-like particles to deliver up to 36 kB DNA to selected cells in the body\n\nHis laboratory is very inter disciplinary\, combining biophysical studies\, directed evolution and biom edical applications — all held together by protein engineering.\n\nWebsi te:\nhttps://plueckthun.bioc.uzh.ch\n  LOCATION:MED 0 1618 https://plan.epfl.ch/?room==MED%200%201618 STATUS:CONFIRMED END:VEVENT END:VCALENDAR