Varun Gadkari
University of Minnesota, MN·Biophysics
A growing share of modern medicines are not small chemicals but large, fragile molecules: antibodies, messenger RNA drugs, and viruses repurposed as gene-delivery vehicles. Whether they work depends on keeping their three-dimensional shape intact through manufacturing, shipping, storage, and injection.
- Fields
Biophysics
Chemistry
Biochemistry
- Topics
native mass spectrometry
ion mobility mass spectrometry
charge detection mass spectrometry
- Grants
- 1 known grant, through Feb 2031
What they work on
- Map how antibody sequence, glycosylation (attached sugar chains), and aggregation govern stability using native and ion mobility-mass spectrometry, and link these structural features to changes in antigen binding.
- Establish the first mass spectrometry assays that quantify unfolding transitions of kilobase-scale RNA transcripts, and test how encapsulation in lipid nanoparticles alters their stability.
- Define the molecular pathways by which adeno-associated virus capsids destabilize and eject their genomes, comparing serotypes, genomes, and formulations using charge detection mass spectrometry and computational models.
- Benchmark gas-phase stability measurements against solution-phase methods, differential scanning fluorimetry and circular dichroism spectroscopy, to connect structural descriptors to real unfolding and aggregation events.
More about the research
Small structural changes can silence a drug's activity or make the immune system attack it. The stability tests used today report when a molecule melts or loses activity overall, but they cannot say which part of the structure gave way or by what route, so it stays difficult to explain why a given formulation fails.
Why it matters
Antibody, mRNA, and gene-therapy medicines can lose potency or provoke immune reactions when their structures degrade during manufacturing, storage, or delivery. Measurement tools that pinpoint how and where a given biologic falls apart could help developers choose more resilient designs and formulations, making the production and distribution of these treatments more reliable.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Francisco Fernandez-Lima
Florida International University, FL·Chemistry
Develop mass spectrometry workflows that combine solution labeling, trapped ion mobility spectrometry (which separates ions by shape) and electron- or UV-based fragmentation to study biomolecular complexes near their native state.
Joseph Zaia
Boston University, MA·Chemistry
Identify glycosaminoglycans (GAGs), long sulfated sugar chains, attached to specific brain matrisome proteins, using an Omnitrap mass spectrometry platform to analyze peptides carrying several sugar chains.
Carlos Larriba Andaluz
Purdue University, IN·Chemistry
Develop higher-order ion mobility approximations using two-temperature theory, then add ion energy calculations and inelastic collision effects to explain how ion mobility spectrometry separates isomers.
The school
University of Minnesota: 88 labs on PI Pages, $1.4B a year on research, 722 research doctorates a year.
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