Barbara Imperiali
· Class of 1922 ProfessorMassachusetts Institute of Technology · Chemistry
Active 1981–2026
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About
Barbara Imperiali is the Class of 1922 Professor of Chemistry and Biology at MIT. Her research group employs a multidisciplinary approach involving synthesis, state-of-the-art spectroscopy, molecular modeling, enzymology, and molecular biology to address fundamental problems at the interface of chemistry and biology. A primary focus of her work is on protein structure, function, and design, with particular emphasis on understanding enzyme-catalyzed protein glycosylation, especially N-linked glycosylation. Her group investigates the enzymatic processes involved in glycosylation, including the assembly of glycosyl donors and the action of oligosaccharyl transferase (OTase), aiming to develop inhibitors to probe glycosylation roles in pathogenic bacteria and to analyze active OTases from prokaryotic sources. Additionally, her research involves designing and synthesizing chemical tools such as fluorescent and luminescent probes to study complex biological systems, with a focus on protein kinases and signal transduction pathways. These efforts include developing probes for monitoring protein phosphorylation, protein-protein interactions, and cellular activities related to cell migration and cell cycle control. Her work ultimately aims to create chemical probes that elucidate the spatial and temporal dynamics of proteins in cellular pathways, contributing to a deeper understanding of biological processes at the molecular level.
Research topics
- Biochemistry
- Computational biology
- Genetics
- Chemistry
- Biology
- Crystallography
- Nanotechnology
- Optics
- Biophysics
Selected publications
Lanthanide-Binding Tags for 3D X-ray Imaging of Proteins in Cells at Nanoscale Resolution
Journal of the American Chemical Society · 2020 · 50 citations
We report the application of lanthanide-binding tags (LBTs) for two- and three-dimensional X-ray imaging of individual proteins in cells with a sub-15 nm beam. The method combines encoded LBTs, which are tags of minimal size (ca. 15-20 amino acids) affording high-affinity lanthanide ion binding, and X-ray fluorescence microscopy (XFM). This approach enables visualization of LBT-tagged proteins while simultaneously measuring the elemental distribution in cells at a spatial resolution necessary fo…
Strategies and Tactics for the Development of Selective Glycan-Binding Proteins
ACS Chemical Biology · 2021 · 39 citations
Senior authorCorrespondingThe influences of glycans impact all biological processes, disease states, and pathogenic interactions. Glycan-binding proteins (GBPs), such as lectins, are decisive tools for interrogating glycan structure and function because of their ease of use and ability to selectively bind defined carbohydrate epitopes and glycosidic linkages. GBP reagents are prominent tools for basic research, clinical diagnostics, therapeutics, and biotechnological applications. However, the study of glycans is hindere…
Proceedings of the National Academy of Sciences · 2021 · 29 citations
The monotopic phosphoglycosyl transferase (monoPGT) superfamily comprises over 38,000 nonredundant sequences represented in bacterial and archaeal domains of life. Members of the superfamily catalyze the first membrane-committed step in en bloc oligosaccharide biosynthetic pathways, transferring a phosphosugar from a soluble nucleoside diphosphosugar to a membrane-resident polyprenol phosphate. The singularity of the monoPGT fold and its employment in the pivotal first membrane-committed step al…
eLife · 2023-11-24 · 9 citations
articleOpen accessSenior authorBacterial cell surface glycoconjugates are critical for cell survival and for interactions between bacteria and their hosts. Consequently, the pathways responsible for their biosynthesis have untapped potential as therapeutic targets. The localization of many glycoconjugate biosynthesis enzymes to the membrane represents a significant challenge for expressing, purifying, and characterizing these enzymes. Here, we leverage cutting-edge detergent-free methods to stabilize, purify, and structurally…
Biochemistry · 2023-12-18 · 8 citations
articleOpen accessSenior authorCorrespondingThe Campylobacter genus of Gram-negative bacteria is characterized by the expression of N-linked protein glycosylation (pgl) pathways. As Campylobacter concisus is an emerging human pathogen, a better understanding of the variation of the biosynthetic pathways across the genus is necessary to identify the relationships between protein glycosylation and disease. The pgl pathways of C. concisus strains have been reported to diverge from other Campylobacter in steps after the biosynthesis of N-acet…
Recent grants
Development of multifunctional probes for profiling microbial glycans
NIH · $1.4M · 2018–2022
NIH · $1.8M · 2019
NIH · $489k · 1993
Frequent coauthors
- 53 shared
Karen N. Allen
- 33 shared
Greg J. Dodge
Massachusetts Institute of Technology
- 31 shared
Mark M. Chen
Massachusetts Institute of Technology
- 27 shared
Harald Schwalbe
Goethe University Frankfurt
- 25 shared
Christopher W. Reid
Bryant University
- 25 shared
Jacek Stupak
National Research Council Canada
- 22 shared
Langdon J. Martin
Warren Wilson College
- 22 shared
Alyssa J. Anderson
Massachusetts Institute of Technology
Education
- 1983
PhD, Chemistry
Massachusetts Institute of Technology
- 1979
BSc (Hon. First class) Medicinal Chemistry, Chemistry
University College London
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