Shelli Frey
G. Bowers and Louise Hook Mansdorfer Professorship in Chemistry & Professor
Chemistry & Biochemistry
Contact
Address
Room 356
300 North Washington St.
Gettysburg, PA 17325-1400
Education
BS Haverford College, 2001
MS University of Chicago, 2003
PhD University of Chicago, 2008
Academic Focus
biophysical chemistry; lipid membrane biophysics
RESEARCH INTERESTS
Research in my lab is biophysical in nature – essentially using physical and chemical techniques to answer biological questions about the cell membrane, the selectively phosholipid bilayer permeable structure that separates a cell’s interior from its surroundings. We use two-dimensional lipid monolayers at the air/water interface as models of the outer leaflet of the cell membrane that allow control over composition and surface density of the biological components. In addition to monolayers, we create and image with fluorescence microscopy more physiologically relevant giant unilamellar vesicles, essentially spherical lipid bilayers that model a cell membrane without any cellular contents. With access to several cell membrane models and a variety of biophysical techniques, current projects in Lipid lab focus on studying basic intermolecular interactions between the phospholipids contained in the layer and measuring interactions of exogenous biological agents (huntingtin protein, detergents, and nanoparticles are examples) with the cell membrane – including how the agent affects the membrane and how the membrane affects the agent.
RECENT PUBLICATIONS (* denotes Gettysburg College student)
- N Nanajkar, A Sahoo, SL Frey, S Matysiak. Investigating curvature sensing by the Nt17 domain of Huntingtin protein. ACS Chemical Neuroscience, in press.
- H Park, J Gilbert, SL Frey, T Nylander, JA Jackman. Absorption and spreading of sponge-phase lipid nanoparticles on SiO2 and TiO2 surfaces: Ion-specific effects and particle structure. Langmuir, 2025, 41, 4113-4125.
- N Gooran, SW Tan, SL Frey, JA Jackman. Unraveling the biophysical mechanisms of how antiviral detergents disrupt supported lipid membranes: Toward replacing Triton X‑ Langmuir, 2024, 40, 6524-6536.
- A Skeens, JM Markle*, SL Frey#, and J Legleiter#. Divalent cations promote huntingtin fibril formation on endoplasmic reticulum membranes. BBA:Biomembranes, 2024, 1866, 184339.
- A Skeens, C Siriwardhana, SE Massinople, MM Wunder, KM Keith, T Girman, ZL Ellis, SL Frey, and J Legleiter. The polyglutamine domain is the primary driver of seeding in Huntingtin aggregation. PLOS One, 2024, 19(3), e0298323.
RECENT EXTERNAL FUNDING
- National Science Foundation Major Research Instrument Grant: Acquisition of spinning disc confocal microscope for use across three institutions. August 2024
- Procter & Gamble Fund’s Higher Education Grant: Evolving our Biochemistry and Chemistry Curricula: Increasing experiential learning and interdisciplinary thinking, January 2021 – present.
Courses Taught
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Article Absorption and spreading of sponge-phase lipid nanoparticles on SiO2 and TiO2 surfaces: Ion-specific effects and particle structure. Langmuir, 2025, 41, 4113-4125.
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Article Unraveling the biophysical mechanisms of how antiviral detergents disrupt supported lipid membranes: Toward replacing Triton X?100. Langmuir, 2024, 40, 6524-6536.
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Article Divalent cations promote huntingtin fibril formation on endoplasmic reticulum membranes. BBA:Biomembranes, 2024, 1866, 184339.
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Article The polyglutamine domain is the primary driver of seeding in Huntingtin aggregation. PLOS One, 2024, 19(3), e0298323.
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Article Bending rigidity of charged bilayer membranes. Soft Matter, 2019, 15, 6006-6013.