Alanna Schepartz

University of California, Berkeley


Primary Section: 14, Chemistry
Secondary Section: 21, Biochemistry
Membership Type: Member (elected 2014)

Biosketch

Alanna Schepartz is the Milton Harris ’29 PhD Professor of Chemistry and Professor of Molecular, Cellular, and Developmental Biology at Yale University. Schepartz is a chemist recognized for the creative application of chemical synthesis and principles to understand and control biological recognition and function. Her research has contributed to and shaped thinking in multiple areas, including the molecular mechanisms of protein-DNA recognition and transcriptional activation; protein design and engineering and their application to synthetic biology; and the mechanisms by which chemical information is trafficked across biological compartments. She is known in particular for her design of β-peptide bundles, the first and only example of a protein-like architecture that lacks even a single α-amino acid. Schepartz was born in 1962 and raised in New York City. After receiving a BS degree in Chemistry from the State University of New York-Albany in 1982, Schepartz carried out graduate work at Columbia University and postdoctoral work at the California Institute of Technology. She joined the faculty at Yale University in 1988.

Research Interests

Alanna Schepartz’s laboratory studies protein interactions. Her approach is to design molecules that nature does not synthesize–miniature proteins, β-peptides, β-peptide bundles, and pro-fluorescent cell-permeable ligands–which, by virtue of their structure or function, are uniquely suited to address otherwise difficult questions in biology or medicine. Current topics of interest include the creation of miniature proteins to create or rewire cell signaling networks for application in synthetic biology, the development of novel chemical strategies for improved super-resolution imaging of proteins, lipids, and organelles, the design of β-peptides that selfassemble into protein-like quaternary folds devoid of α-amino acids but possessing catalytic function, the mechanism by which peptides and their mimetics traffic across cellular membranes, and the application of small molecule fluorescence strategies to detect posttranslational modifications, protein-protein complexes, and altered protein conformational states inside live cells.

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