Professional Education

  • Ph.D., Georgia Institute of Technology, Chemical & Biomolecular Engineering (2024)
  • B.S., University of Rhode Island, Chemical Engineering (2018)

Stanford Advisors

Contact

  • Academic
    meganmcs@stanford.edu
    University - Scholar Department: Bioengineering Position: Postdoctoral Scholar

Additional Info

All Publications

  • Construction of an Array of Biosensors Using Density Evolution for MicroRNA Monitoring IEEE TRANSACTIONS ON MOLECULAR BIOLOGICAL AND MULTI-SCALE COMMUNICATIONS Sethuraman, M. G., McSweeney, M. A., Styczynski, M. P., Fekri, F. 2025; 11 (3): 335-343

    View details for DOI 10.1109/TMBMC.2025.3547892

    View details for Web of Science ID 001574824000008

  • A modular cell-free protein biosensor platform using split T7 RNA polymerase SCIENCE ADVANCES Mcsweeney, M. A., Patterson, A. T., Loeffler, K., de Larrea, R., Mcnerney, M. P., Kane, R. S., Styczynski, M. P. 2025; 11 (8): eado6280

    Abstract

    Conventional laboratory protein detection techniques are not suitable for point-of-care (POC) use because they require expensive equipment and laborious protocols, and existing POC assays suffer from long development timescales. Here, we describe a modular cell-free biosensing platform for generalizable protein detection that we call TLISA (T7 RNA polymerase-linked immunosensing assay), designed for extreme flexibility and equipment-free use. TLISA uses a split T7 RNA polymerase fused to affinity domains against a protein. The target antigen drives polymerase reassembly, inducing reporter expression. We characterize the platform and then demonstrate its modularity by using 16 affinity domains against four different antigens with minimal protocol optimization. We show that TLISA is suitable for POC use by sensing human biomarkers in serum and saliva with a colorimetric readout within 1 hour and by demonstrating functionality after lyophilization. Altogether, this technology has the potential to enable truly rapid, reconfigurable, modular, and equipment-free detection of diverse classes of proteins.

    View details for DOI 10.1126/sciadv.ado6280

    View details for Web of Science ID 001428018300002

    View details for PubMedID 39982986

    View details for PubMedCentralID PMC11844732

https://orcid.org/0000-0001-5012-3218