Title:
Reprogramming the Immune Response Through Biomolecular Engineering

dc.contributor.author Spangler, Jamie
dc.contributor.corporatename Georgia Institute of Technology. School of Chemical and Biomolecular Engineering en_US
dc.contributor.corporatename Johns Hopkins University. School of Medicine en_US
dc.contributor.corporatename Johns Hopkins University. Department of Biomedical Engineering en_US
dc.date.accessioned 2021-10-29T23:41:56Z
dc.date.available 2021-10-29T23:41:56Z
dc.date.issued 2021-10-20
dc.description Presented on October 20, 2021 from 3:30 p.m.- 4:30 p.m. at the College of Computing 16, Georgia Tech, Atlanta, GA. en_US
dc.description Dr. Jamie Spangler earned a Bachelor of Science degree in Biomedical Engineering at Johns Hopkins University and went on to conduct her Ph.D. research in Biological Engineering in Professor K. Dane Wittrup’s group at MIT, studying antibody-mediated down-regulation of epidermal growth factor receptor as a new mechanism for cancer therapy. She then completed a postdoctoral fellowship in Professor K. Christopher Garcia’s lab in the Molecular & Cellular Physiology and Structural Biology departments at Stanford University School of Medicine, focusing on engineering cytokine systems to bias immune homeostasis. Dr. Spangler launched her independent research group at Johns Hopkins University in July 2017, jointly between the departments of Biomedical Engineering and Chemical & Biomolecular Engineering. Her lab, located in the Translational Tissue Engineering Center at the School of Medicine, applies structural and mechanistic insights to re-engineer existing proteins and design new proteins that therapeutically modulate the immune response. en_US
dc.description Runtime: 66:16 minutes en_US
dc.description.abstract The repertoire of naturally occurring proteins is finite and many molecules induce multiple confounding effects, limiting their efficacy as therapeutics. Recently, there has been a growing interest in redesigning existing proteins or engineering entirely new proteins to address the deficiencies of molecules found in nature. Researchers have traditionally taken an unbiased approach to protein engineering, but as our knowledge of protein structure-function relationships advances, we have the exciting opportunity to apply molecular principles to guide engineering. Leveraging cutting-edge tools and technologies in structural biology and molecular design, our lab is pioneering a unique structure-based engineering approach to elucidate the mechanistic determinants of protein activity, in order to inform therapeutic development. Our group is particularly interested in engineering immune proteins, such as cytokines, growth factors, and antibodies, to bias the immune response for targeted disease treatment. Despite the recent explosive growth of protein drugs within the pharmaceutical market, limitations such as delivery, acquired resistance, and toxicity have impeded realization of the full potential of these therapeutics, necessitating new approaches that synergize with existing strategies to address clinically unmet needs. This talk will highlight ongoing work in our lab that spans the discovery, design, and translation of novel molecular immunotherapeutics for applications ranging from cancer to autoimmune disorders to regenerative medicine. en_US
dc.format.extent 66:16 minutes
dc.identifier.uri http://hdl.handle.net/1853/65406
dc.language.iso en_US en_US
dc.publisher Georgia Institute of Technology en_US
dc.relation.ispartofseries School of Chemical and Biomolecular Engineering Seminar Series
dc.subject Molecular engineering en_US
dc.subject Immunology en_US
dc.subject Therapeutic proteins en_US
dc.title Reprogramming the Immune Response Through Biomolecular Engineering en_US
dc.type Moving Image
dc.type.genre Lecture
dspace.entity.type Publication
local.contributor.corporatename School of Chemical and Biomolecular Engineering
local.contributor.corporatename College of Engineering
local.relation.ispartofseries School of Chemical and Biomolecular Engineering Seminar Series
relation.isOrgUnitOfPublication 6cfa2dc6-c5bf-4f6b-99a2-57105d8f7a6f
relation.isOrgUnitOfPublication 7c022d60-21d5-497c-b552-95e489a06569
relation.isSeriesOfPublication 388050f3-0f40-4192-9168-e4b7de4367b4
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