Genetically encoded sensors provide unique advantages for monitoring biological analytes with molecular and cellular-level specificity. While sensors derived from fluorescent proteins represent staple tools in biological imaging, these probes are limited to optically accessible preparations owing to physical curbs on light penetration. In contrast to optical methods, magnetic resonance imaging (MRI) may be used to noninvasively look inside intact organisms at any arbitrary depth and over large fields of view. These capabilities have spurred the development of innovative methods to connect MRI readouts with biological targets using protein-based probes that are in principle genetically encodable. Here, we highlight the state-of-the-art in MRI-based biomolecular sensors, focusing on their physical mechanisms, quantitative characteristics, and biological applications. We also describe how innovations in reporter gene technology are creating new opportunities to engineer MRI sensors that are sensitive to dilute biological targets.
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http://dx.doi.org/10.1002/anse.202200019 | DOI Listing |
Analyst
January 2025
College of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou, 310018, China.
A novel electrochemical microsensor was constructed on a traditional acupuncture needle (AN) and used to monitor a biomarker of the SARS-CoV-2-N protein. The reversible interaction of the borate bond between the -diol in this glycoprotein and the phenylboronic acid in 4-mercaptophenylboronic acid (4-MPBA) was accomplished. This interaction was applied to anchor the SARS-CoV-2-N protein onto 4-MPBA, which was covalently self-assemblied onto electrodeposited AuNPs by the S-Au bond.
View Article and Find Full Text PDFInt J Mol Sci
January 2025
Department of Life Sciences, POSTECH Biotech Center, Pohang University of Science and Technology, 77 Cheongam-ro, Nam-gu, Pohang-si 37673, Republic of Korea.
The emergence of numerous SARS-CoV-2 variants, characterized by mutations in the viral RNA genome and target proteins, has presented challenges for accurate COVID-19 diagnosis. To address this, we developed universal aptamer probes capable of binding to the spike proteins of SARS-CoV-2 variants, including highly mutated strains like Omicron. These aptamers were identified through protein-based SELEX using spike proteins from three key variants (D614G-substituted Wuhan-Hu-1, Delta, and Omicron) and virus-based SELEX, known as viro-SELEX.
View Article and Find Full Text PDFNat Commun
January 2025
School of Food and Biological Engineering, Engineering Research Center of Bio-process, Ministry of Education, Key Laboratory of Animal Source of Anhui Province, Hefei University of Technology, Hefei, 230009, China.
Dissection of the physiological interactomes of histone post-translational modifications (hPTMs) is crucial for understanding epigenetic regulatory pathways. Peptide- or protein-based histone photoaffinity tools expanded the ability to probe the epigenetic interactome, but in situ profiling in native cells remains challenging. Here, we develop a nucleus-targeting histone-tail-based photoaffinity probe capable of profiling the hPTM-mediated interactomes in native cells, by integrating cell-permeable and nuclear localization peptide modules into an hPTM peptide equipped with a photoreactive moiety.
View Article and Find Full Text PDFiScience
December 2024
Department of Molecular Environmental Biotechnology, Helmholtz-Centre for Environmental Research - UFZ, 04318 Leipzig, Saxony, Germany.
Protein-based stable isotope probing (protein-SIP) can link microbial taxa to substrate assimilation. Traditionally, protein-SIP requires a sample-specific metagenome-derived database for samples with unknown composition. Here, we describe GroEL-prototyping-based stable isotope probing (GroEL-SIP), that uses GroEL as a taxonomic marker protein to identify bacterial taxa (GroEL-proteotyping) coupled to SIP directly linking identified taxa to substrate consumption.
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