An osmium-coated lensed fiber (OLF) probe combined with a silver-coated black silicon (SBS) substrate was used to generate a dielectrophoretic (DEP) force that traps bacteria and enables Raman signal detection from bacteria. The lensed fiber coated with a 2-nm osmium layer was used as an electrode for the DEP force and also as a lens to excite Raman signals. The black silicon coated with a 150-nm silver layer was used both as the surface-enhanced Raman scattering (SERS) substrate and the counter electrode. The enhanced Raman signal was collected by the same OLF probe and further analyzed with a spectrometer. For Raman measurements, a drop of bacterial suspension was placed between the OLF probe and the SBS substrate. By controlling the frequency of an AC voltage on the OLF probe and SBS substrate, a DEP force at 1 MHz concentrated bacteria on the SBS surface and removed the unbound micro-objects in the solution at 1 kHz. A bacteria concentration of 6 × 10 CFU/mL (colony forming units per mL) could be identified in less than 15 min, using a volume of only 1 μL, by recording the variation of the Raman peak at 740 cm.
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http://dx.doi.org/10.1016/j.bios.2021.113463 | DOI Listing |
bioRxiv
August 2024
School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta, GA.
Myocilin-associated glaucoma is a protein-conformational disorder associated with formation of a toxic amyloid-like aggregate. Numerous destabilizing single point variants, distributed across the myocilin olfactomedin β-propeller (OLF, myocilin residues 245-504, 30 kDa) are associated with accelerated disease progression. , wild type (WT) OLF can be promoted to form thioflavin T (ThT)-positive fibrils under mildly destabilizing (37°C, pH 7.
View Article and Find Full Text PDFNat Commun
January 2024
School of Chemistry & Biochemistry, Georgia Institute of Technology, Atlanta, USA.
Studies of folded-to-misfolded transitions using model protein systems reveal a range of unfolding needed for exposure of amyloid-prone regions for subsequent fibrillization. Here, we probe the relationship between unfolding and aggregation for glaucoma-associated myocilin. Mutations within the olfactomedin domain of myocilin (OLF) cause a gain-of-function, namely cytotoxic intracellular aggregation, which hastens disease progression.
View Article and Find Full Text PDFMicrobiol Spectr
December 2023
Ottawa Laboratory (Fallowfield), Canadian Food Inspection Agency , Ottawa, Ontario, Canada.
Human listeriosis is caused by consuming foods contaminated with the bacterial pathogen , leading to the development of a severe and life-threatening foodborne illness. Detection of present in food and food processing environments is crucial for preventing infection. The peptidoglycan hydrolase IspC anchors non-covalently to the bacterial surface through its C-terminal cell wall-binding domain (CWBD), CWBD.
View Article and Find Full Text PDFBiosens Bioelectron
November 2021
Department of Mechanical Engineering, School of Engineering, The University of Tokyo, Tokyo, 113-8656, Japan. Electronic address:
ACS Chem Biol
February 2014
School of Chemistry & Biochemistry, Georgia Institute of Technology, 901 Atlantic Drive NW, Atlanta, Georgia 30332-0400, United States.
Mutations in the olfactomedin domain of myocilin (myoc-OLF) are the strongest link to inherited primary open angle glaucoma. In this recently identified protein misfolding disorder, aggregation-prone disease variants of myocilin hasten glaucoma-associated elevation of intraocular pressure, leading to vision loss. Despite its well-documented pathogenic role, myocilin remains a domain of unknown structure or function.
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