President, SRI Biosciences Division
Kathlynn Brown currently serves as President of SRI’s Biosciences Division. She joined SRI in 2014, and in 2021 became Vice President of Drug Delivery Systems before becoming SRI Biosciences’ President in 2023.
Brown is a recognized leader in life sciences with over 50 peer-reviewed papers, reviews, and book chapters. She has a proven track record for developing groundbreaking research in organic chemistry, peptide chemistry, biochemistry, and molecular biology to address challenges in biomedical research. In her eight-year tenure at SRI, Brown has helped the organization double down on its impacts in these fields.
Brown obtained her PhD in organic chemistry at the University of Texas at Austin, during which time she received fellowships from the Mahler Memorial Foundation and the Organic Division of the American Chemical Society. She continued her training at the University of California at San Francisco, where she was a Damon Runyon Walter Winchell Postdoctoral Fellow.
Brown began her independent career at UT Southwestern Medical Center and moved to SRI to expand her translational research. Under her leadership as SRI’s Vice President of Drug Delivery, Brown developed FOX Three™ and DiaCyt™, two of SRI’s flagship internal research and development projects that have yielded important commercial collaborations. Brown also effectively managed work at SRI’s Shenandoah Valley site, growing the team and capabilities, as well as engaging with pharmaceutical companies.
Her laboratory was among the first to adopt cell-based biopanning of phage-displayed peptide libraries. Using this approach, she has developed a suite of high-affinity peptides that target a variety of different cell types. Brown has co-authored numerous peer-reviewed papers, three reviews, and one book chapter in this area.
View Kathlynn Brown’s publications.
Recent publications
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Tumor-specific intracellular delivery: peptide-guided transport of a catalytic toxin
Here we optimize our lead peptide by a series of chemical modifications including truncations, N-terminal capping, and changes in valency.
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Introduction of plasmid encoding for rare tRNAs reduces amplification bias in phage display biopanning
Here we present a method that reduces amplification bias by addition of a plasmid that encodes six low abundance tRNAs into K91 Escherichia coli.
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Identification of a Novel Lysosomal Trafficking Peptide Using Phage Display Biopanning Coupled with Endocytic Selection Pressure
We performed phage display biopanning on cancer cells that are treated with selective inhibitors of a given mechanism of endocytosis.