Brandon Bordeau
University of Michigan, MI·Pharmacology
Antibody-drug conjugates (ADCs) are medicines that attach a toxic drug to an antibody so the antibody can deliver it to target cells, such as cancer cells. Despite great interest, 89% of ADCs fail in clinical trials, most often because a dose strong enough to work is too toxic.
- Fields
Pharmacology
Biomedical Engineering
Engineering
- Topics
antibody-drug conjugates
antibody drug complex
ADCx
- Grants
- 1 known grant, through Nov 2029
What they work on
- Compare a lead anti-HER2 anti-MMAE antibody drug complex (ADCx) with the standard antibody-drug conjugate trastuzumab-vc-MMAE in mice, measuring drug distribution, tumor-fighting efficacy and tolerability.
- Identify which antibody and drug properties best improve ADCx safety and efficacy, building on the pharmacokinetic model-informed antibody engineering used to design the lead complex.
- Discover and optimize anti-drug antibodies against new payloads, prioritizing drugs with many uses, to build a modular ADCx panel whose cell-targeting part can be easily swapped.
More about the research
The toxicity mainly comes from the linker payload, the chemical link and drug attached to the antibody, which can release the drug in the wrong places. Years of efforts to redesign linkers and payloads have struggled, because fixing one problem often creates another.
Why it matters
Antibody-drug conjugates often fail or cause side effects that force patients to delay, reduce or stop treatment. A drug-delivery format that avoids the problematic chemical linker could widen the gap between effective and toxic doses. Because the targeting part can be swapped, the same approach could eventually be adapted to treat cancer, autoimmune disease and infectious disease.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Lawrence Tumey
Binghamton University, NY·Chemistry
Design new self-immolative spacers, extending the GlyPro spacer, that release ADC payloads lacking amine handles, such as sulfonamides, ureas, carbamates and hydroxamates.
Sabine Brouxhon
University of Rochester, NY·Pharmacology
Characterize how soluble E-cadherin (sEcad) binds and activates the IGF-1R growth receptor, using purified IGF-1R holoreceptor and biochemical and biophysical binding and phosphorylation measurements, including synergy with the natural ligands IGF-1 and EGF.
Reza Abdi
University of California-Los Angeles, CA·Microbiology & Immunology
Optimize the stability, binding and body distribution of nanoparticles carrying an antibody against PNAd, a molecule found only on high endothelial venules, in NOD mice that develop type 1 diabetes.
The school
University of Michigan: 124 labs on PI Pages, $2.1B a year on research, 963 research doctorates a year.
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