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Benjamin Brown, M.D., Ph.D.

  • Assistant Professor of Pharmacology

Phone

615-322-2861

Email

benjamin.p.brown@vanderbilt.edu
Vanderbilt University
465 21st Ave S
Nashville, TN 37212

Benjamin Brown, M.D., Ph.D.

  • Assistant Professor of Pharmacology

615-322-2861

benjamin.p.brown@vanderbilt.edu

Vanderbilt University
465 21st Ave S
Nashville, TN 37212

Profile

I am an Assistant Professor in the Department of Pharmacology and Center for Applied AI in Protein Dynamics at Vanderbilt University. My research is focused on the development and application of methods in computational chemistry and deep learning for biomolecular modeling and computer-aided drug design (CADD). In the pursuit of new targeted therapies for cancer, I employ a multi-pronged approach: (i) detailed molecular modeling and simulation of cancer-associated protein variants, such as oncogenic EGFR kinase domain variants with and without acquired resistance mutations, to determine the essential dynamics differentiating wild-type and mutant function; (ii) application of ligand- and structure-based CADD methods, including conventional methods and deep learning, to study the determinants of drug action and screen for new compounds ; and (iii) the development of new algorithms to address shortcomings in (ii) as we seek to target proteins studied in (i). The methods that I develop and apply are broadly relevant to multiple proteins and potential therapeutic targets, such that advances we make in cancer investigations may be applied in other basic and translational investigations.

After I finished my BS in Chemistry and Neuroscience at Baldwin Wallace University in Berea, OH, I began medical school at Vanderbilt University School of Medicine through the Medical Scientist Training Program. I completed my PhD training in the laboratory of Jens Meiler, PhD and collaborated extensively with Christine Lovly, MD, PhD as part of the Personalized Structural Biology Program’s work with the Vanderbilt-Ingram Cancer Center. Some of our work includes having proposed a structural mechanism of resistance conferred by the G724S mutation in EGFR exon 19 deletion mutations, and demonstrating that the landscape of potential acquired resistance mutations available to a protein is dependent on the specific underlying activating mutation(s). We have also demonstrated that the clinically synonymous “exon 19 deletion” variants of EGFR are in fact a heterogeneous group of mutations with varying activation profiles, enzyme kinetics, and inhibitor sensitivities.

Education

  • M.D.,Vanderbilt University, Nashville, Tennessee (2023)
  • Ph.D., Vanderbilt University, Nashville, Tennessee (2022)
  • B.S., Baldwin Wallace University, Cleveland, Ohio (2015)

Research Emphasis

Publications

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