Heidelberg, Germany

Affimed Therapeutics

www.affimed.com
Heidelberg, Germany

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Grant
Agency: European Commission | Branch: FP7 | Program: MC-ITN | Phase: FP7-PEOPLE-2012-ITN | Award Amount: 3.53M | Year: 2012

In the research part we will deal with the basic principles of the innate immune defense used to control tumors and viral infections with a focus on NK and NK/T cells, including analysis of NK receptor genomics/epigenetics, gene polymorphisms/disease linkage, differentiation of hitherto unrecognized NK cell subpopulations and novel ligands for NK receptors exposed by tumor and/or virally infected cells. We will investigate the mechanisms installed by tumors and viruses to avoid or subvert immune defenses. This will include the investigation of the role of NK/T cell subpopulations in the defense against tumors and infections by herpes virus family members, some being involved in tumor formation, in the development of inflammatory diseases and/or constituting a frequent complication during tumor therapy. The project will support anti-tumor and anti-viral therapies by developing novel technology for NK cell generation from cord blood stem cells for NK cell infusions in patients, by genetic engineering of NK cells and by using NK receptors and their ligands to develop novel reagents for amplifying anti-tumor and -viral activities of NK/T cells. It will further undertake basic studies on the potential of the newly emerging iPS cell technology for reconstituting immune systems including NK cells in patients with hematologic cancers. All students of this ITN will be trained in state-of-the-art immunotechnology including wider aspects of molecular medicine at the individual partner universities. An exchange of students between the different partners will be organized to ensure that every participant will be trained in several laboratories/universities with different expertise. It will further include network-wide training modules with cutting-edge lectures of internationally recognized research experts in the field, state-of-the-art seminars in the front-line technologies used in this project as well as courses in genome-wide bioinformatics, business and patent rights.


McAleese F.,Affimed Therapeutics | Eser M.,Affimed Therapeutics
Future Oncology | Year: 2012

Tandem diabodies (TandAbs®) are tetravalent bispecific molecules comprised of antibody variable domains with two binding sites for each antigen. RECRUIT-TandAbs can simultaneously engage an immune system effector cell, such as a natural killer cell or a cytotoxic T cell, and an antigen expressed specifically on a cancer cell, thus leading to killing of the cancer cell. Recruitment of immune effector cells is highly specific and mediated via binding of the TandAb to molecules expressed on the surface of these cells. Furthermore, the absence of an Fc domain allows TandAbs to avoid certain IgG-mediated side effects. With a molecular weight of approximately 110 kDa, TandAbs are far above the first-pass renal clearance limit, offering a pharmacokinetic advantage compared with smaller bispecific antibody formats. This article reviews the RECRUIT-TandAb technology and the therapeutic potential of these molecules. © 2012 Future Medicine Ltd.


Patent
Affimed Therapeutics | Date: 2011-10-05

In one aspect, the present invention relates to an antigen-binding molecule specific for albumin and CD3 comprising two polypeptide chains, each polypeptide chain having at least four variable domains in an orientation preventing Fv formation and the two polypeptide chains are dimerized with one another thereby forming a multivalent antigen-binding molecule. On each of the two polypeptide chains the four variable domains are arranged in the order V_(L)A-V_(H)B-V_(L)B-V_(H)A from the N-terminal to the C-terminal of the polypeptide. Compositions of the antigen-binding molecule and the methods of using the antigen-binding molecule or the compositions thereof for treatment of various diseases are also provided herein.


Patent
Affimed Therapeutics | Date: 2012-05-09

The present invention relates to binding molecules that specifically bind to the human Fc gamma receptor expressed on the surface of natural killer (NK) cells and macrophages (i.e. FcRIIIA), and in particular binding molecules that specifically bind the A form FcRIII but do not bind to the B form of FcRIII, as well as to the use of such binding molecules in the diagnosis and treatment of disease. The invention further extends to polynucleotides encoding such binding molecules, host cells comprising such polynucleotides and methods of producing binding molecules of the invention using such host cells.


Patent
Affimed Therapeutics | Date: 2015-10-14

The invention relates to a trispecific antigen-binding polypeptide dimer comprising a first polypeptide and a second polypeptide, each polypeptide having at least four domains of immunoglobulin chain variable regions linked one after another, wherein two of said four antigen binding sites are specific for the same antigen and the polypeptide can be used as a medicament for tumor therapy.


Patent
Affimed Therapeutics | Date: 2013-01-11

Described are mono- and multivalent scFv-antibodies comprising the binding sites specific for the human T cell marker CD3. These antibodies are strongly immunosuppressive and do not cause a significant release of cytokines. Furthermore, polynucleotides encoding said antibodies are described as well as vectors comprising said polynucleotides, host cells transformed therewith and their use in the production of said antibodies. Pharmaceutical compositions containing any of the above mentioned polynucleotides, antibodies or vectors are useful for immunotherapy, preferably against acute transplant rejections.


Patent
Affimed Therapeutics | Date: 2016-02-10

The disclosure relates to a humanized CD3 binding site, which comprises (a) a variable heavy chain domain (VH) as depicted in SEQ ID NO:8 and a variable light chain domain (VL) as depicted in SEQ ID NO:3; or (b) a variable heavy chain domain (VH) as depicted in SEQ ID NO:9 and a variable light chain domain (VL) as depicted in SEQ ID NO:4. The CD3 binding sites have an increased stability, while the binding affinity has been retained due to mutations at positions VH111 and VL49.


Patent
Affimed Therapeutics | Date: 2011-08-31

In one aspect, the present invention relates to an antigen-binding molecule comprising two polypeptide chains, each polypeptide chain having at least four variable domains in an orientation preventing Fv formation and the two polypeptide chains are dimerized with one another thereby forming a multivalent antigen-binding molecule. On each of the two polypeptide chains the four variable domains are arranged in the order V_(L)A-V_(H)B-V_(L)B-V_(H)A from the N-terminal to the C-terminal of the polypeptide.. Compositions of the antigen-binding molecule and the methods of using the antigen-binding molecule or the compositions thereof for treatment of various diseases are also provided herein.


News Article | July 1, 2014
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