ORCID Profile
0000-0003-0296-9846
Current Organisation
University of California, Irvine
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Publisher: Wiley
Date: 16-08-2017
Publisher: Wiley
Date: 12-04-2022
Abstract: Unlocking the potential of personalized medicine in point‐of‐care settings requires a new generation of biomarker and proteomic assays. Ideally, assays could inexpensively perform hundreds of quantitative protein measurements in parallel at the bedsides of patients. This goal greatly exceeds current capabilities. Furthermore, biomarker assays are often challenging to translate from benchtop to clinic due to difficulties achieving and assessing the necessary selectivity, sensitivity, and reproducibility. To address these challenges, we developed an efficient ( min), robust (comparatively lower CVs), and inexpensive (decreasing reagent use and cost by %) immunoassay method. Specifically, the immunoblot membrane is dotted with the s le and then developed in a vortex fluidic device (VFD) reactor. All assay steps—blocking, binding, and washing—leverage the unique thin‐film microfluidics of the VFD. The approach can accelerate direct, indirect, and sandwich immunoblot assays. The applications demonstrated include assays relevant to both the laboratory and the clinic.
Publisher: American Chemical Society (ACS)
Date: 30-04-2020
Publisher: Wiley
Date: 25-04-2022
Publisher: American Chemical Society (ACS)
Date: 05-11-2020
Publisher: American Chemical Society (ACS)
Date: 20-06-2023
Publisher: Wiley
Date: 25-04-2022
Publisher: American Chemical Society (ACS)
Date: 26-03-2018
Publisher: American Chemical Society (ACS)
Date: 22-01-2019
Publisher: American Chemical Society (ACS)
Date: 17-04-2020
Publisher: Wiley
Date: 12-04-0006
Abstract: Unlocking the potential of personalized medicine in point‐of‐care settings requires a new generation of biomarker and proteomic assays. Ideally, assays could inexpensively perform hundreds of quantitative protein measurements in parallel at the bedsides of patients. This goal greatly exceeds current capabilities. Furthermore, biomarker assays are often challenging to translate from benchtop to clinic due to difficulties achieving and assessing the necessary selectivity, sensitivity, and reproducibility. To address these challenges, we developed an efficient ( min), robust (comparatively lower CVs), and inexpensive (decreasing reagent use and cost by %) immunoassay method. Specifically, the immunoblot membrane is dotted with the s le and then developed in a vortex fluidic device (VFD) reactor. All assay steps—blocking, binding, and washing—leverage the unique thin‐film microfluidics of the VFD. The approach can accelerate direct, indirect, and sandwich immunoblot assays. The applications demonstrated include assays relevant to both the laboratory and the clinic.
Publisher: Cold Spring Harbor Laboratory
Date: 30-09-2020
DOI: 10.1101/2020.09.29.319145
Abstract: The botulinum neurotoxin serotype A (BoNT/A) cuts a single peptide bond in SNAP25, an activity used to treat a wide range of diseases. Reengineering the substrate specificity of BoNT/A’s protease domain (LC/A) could expand its therapeutic applications however, LC/A’s extended substrate recognition (≈60 residues) challenges conventional approaches. We report a directed evolution method for retargeting LC/A’s substrate and retaining its exquisite specificity. The resultant eight-mutation LC/A (omLC/A) has improved cleavage specificity and catalytic efficiency (1300- and 120-fold, respectively) for SNAP23 versus SNAP25 compared to a previously reported LC/A variant. Importantly, the BoNT/A holotoxin equipped with omLC/A infiltrates neurons and retains its SNAP23 activity. The identification of substrate control loops outside BoNT/A’s active site could guide the design of improved BoNT proteases and inhibitors. Directed evolution of the BoNT/A protease targets a new cellular protein, SNAP23, expanding its therapeutic potential.
No related grants have been discovered for Gregory Weiss.