During the past 18 years, I have discovered and developed novel medicine leads across all of AstraZeneca’s major disease areas: oncology, inflammation, respiratory and metabolism. 

What drives me is applying science and creativity to design new medicines that make a difference for patients. My first degree was in chemical engineering, and I was drawn to the concepts of molecular evolution and protein design and how to make something useful out of them. My PhD, from the Universität Zürich, is in molecular evolution, harnessing the concept of Darwinian evolution to create and evolve new proteins with novel functionality.

I started my biotech career in research in a small biotech company in Cambridge, discovering antibody medicines using those principles, before moving into clinical development as 产品介绍 Development 团队 Leader. I was most recently 产品介绍 Development 团队 Leader and Senior Director, R&D, in CVRM iMed, MedImmune. What motivates me today is knowing just how many people have worked extremely hard and sacrificed so much to make the discoveries that led to a clinical discovery.

At AstraZeneca, I initially continued my work in research to head up the Global Technology Department, and become a discovery platform expert for antibody, protein, peptide and nucleic acid-based biopharmaceuticals. Using design and directed evolution to create drug leads beyond just antibodies resulted in nearly half of the pre-clinical 文件夹 being biologics that were not standard monoclonal antibodies. It also led me to found a synthetic peptide discovery 团队 that worked closely with our colleagues in cardiovascular and metabolism discovery. One of the molecules looked so exciting that, in 2013, I was able to take this peptide into clinical trials and generate the data that could transform it into a new medicine.

As 产品介绍 Development 团队 Leader, my primary role today is to advance candidate drugs for type-2 diabetes, obesity, diabetic nephropathy and non-alcoholic steatohepatitis (NASH), from late-pre-clinical to clinical proof-of-concept, and to transition them to late-stage development. Through my Fellow position at the University of Cambridge, I continue supervising PhD students in a number of protein design and directed evolution projects to stay close to the science that led me onto my journey.

The great thing 关于 creating new medicines is the intellectual work of designing a molecule to attack a disease in such a way that it makes a very significant, meaningful difference to the patient. Being able to demonstrate this first in animal models of the disease and finally in the clinic is incredibly rewarding.

What drives me is applying science and creativity to create new medicines that make a difference for patients.

Lutz Jermutus PhD Head of Projects

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2017 MedImmune President’s Award (project team award)皇冠官网

 

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2015 Honorary Fellow of the Faculty of Pharmaceutical Medicine of the Royal Colleges of Physicians of the United Kingdom皇冠官网

 

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2013 Industrial Fellow of Trinity Hall, University of Cambridge皇冠官网

 


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2009 Fellow of the Royal Society of Chemistry (FRSC) 皇冠官网

 


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1997 Graduate Kekulé Fellowship of Verband der Chemischen Industrie皇冠官网

 


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1991 Undergraduate scholarship of Studienstiftung des deutschen Volkes皇冠官网

 



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Tailoring in vitro evolution for protein affinity or stability.皇冠官网

J. Hanes, L. Jermutus, S. Bornhauser-Weber, H.-R. Bosshard and A. Plückthun. (1998) Ribosome display selects and evolves high-affinity binding antibodies in vitro from immune libraries. Proc. Natl. Acad. Sci. USA 95:14130-14135.

Structure-based chimeric enzymes as an alternative to directed enzyme evolution: phytase as a test case.皇冠官网

L Jermutus, A. Honegger, F. Schwesinger, J.Hanes and A.Plückthun. (2001) Tailoring in vitro evolution for protein affinity or stability. Proc. Natl. Acad. Sci. USA 98:75-80.

Probing a protein-protein interaction by in vitro evolution.皇冠官网

L. Jermutus, M. Tessier, L. Pasamontes, A. P.G.M. van Loon and M. Lehmann. (2001) Structure-based chimeric enzymes as an alternative to directed enzyme evolution: phytase as a test case. J. Biotechnol. 85:15-24.

Harnessing phage and ribosome display for antibody optimisation Trends Biotechnol.皇冠官网

G. Thom, A. Cockroft, A. Buchanan, C. Jobery Candotti, S. Cohen, D. Lowne, P. Monk, C. Shorrock-Hart, L. Jermutus and R. Minter. (2006) Probing a protein-protein interaction by in vitro evolution. Proc. Natl. Acad. Sci. USA 103:7619-7624.

Harnessing phage and ribosome display for antibody optimisation Trends Biotechnol.皇冠官网

P. Dufner, L. Jermutus, R. Minter. (2006) Harnessing phage and ribosome display for antibody optimisation Trends Biotechnol. 24:523-529.

Potent peptide mimetics of human IgG1-Fc.皇冠官网

S. Bonetto, L. Spadola, A. G. Buchanan, L. Jermutus, J. Lund. (2009) Potent peptide mimetics of human IgG1-Fc. FASEB J. 23:575-85.

Challenges and opportunities for non-antibody scaffold drugs Drug Discov.皇冠官网

R. Vazquez-Lombardi, T. G. Phan, C. Zimmermann, D. Lowe, L. Jermutus, D. Christ (2015) Challenges and opportunities for non-antibody scaffold drugs Drug Discov. Today 20:1271-1283.

Combinatorial screening identifies novel promiscuous Matrix Metalloprotease (MMP) activities that lead to inhibition of the therapeutic target IL-13 Chem.皇冠官网

C. Urbach, N. C. Gordon, I. Strickland, C. Joberty-Candotti, D. Lowne, F. Hollfelder, R. R. Minter , L. Jermutus (2015) Combinatorial screening identifies novel promiscuous Matrix Metalloprotease (MMP) activities that lead to inhibition of the therapeutic target IL-13 Chem. Biol. 22:1442-52.

Robust anti-obesity and metabolic effects of a GLP-1/glucagon co-agonist peptide in rodents and non-human primates Diabetes Obes. Metab. 皇冠官网

S. Henderson, A. Konkar, D. Hornigold, M. Fritsch Fredin, R. Jansson-Lofmark, R. Jackson, J. Naylor, A. Rossi, M. Bednarek, N. Bhagroo, H. Salari, S. Will, S. Oldham, G. Hansen, J. Jelsing, H. Cucak, T. Klein, J. Grimsby, S. Maguire, L. Jermutus, C.Rondinone, M. Coghlan (2016) Robust anti-obesity and metabolic effects of a GLP-1/glucagon co-agonist peptide in rodents and non-human primates Diabetes Obes. Metab. 18:1176-1190.

A CD80-biased CTLA4-Ig fusion protein with superior in vivo efficacy at low, infrequent doses by simultaneous engineering of affinity, selectivity, stability and FcRn binding J. Immunol.皇冠官网

J. Douthwaite, J. Moisan,  C. Priventseev, B. Soskic, S. Sabbah, S. Cohen, A. Collinson, E. England, C. Huntington, B. Kemp, L. Zhuang, S. Hudak, G. Rees, D. Goldberg, C. Barton, L. Chang, I. Vainshtein, M. Liang, L. Iciek, P. Ambery, M. Peakman, T. Vaughan, T. Tree, D. Sansom, M. Bowen, R. Minter, L. Jermutus (2017) A CD80-biased CTLA4-Ig fusion protein with superior in vivo efficacy at low, infrequent doses by simultaneous engineering of affinity, selectivity, stability and FcRn binding J. Immunol. 198:528-537. Correction 199:1943.

LEAP2 is an endogenous antagonist of the ghrelin receptor Cell Metab.皇冠官网

X. Ge, H. Yang, M. Bednarek, H. Galon-Tilleman, P. Chen, M. Chen, S. Crawley, J. Lichtman, M. Saberi, H. Tian, L. Jermutus, J. Grimsby, C. Rondinone, D. Kaplan (2018) LEAP2 is an endogenous antagonist of the ghrelin receptor Cell Metab. 27:461-469.

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