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Proteomics01:33

Proteomics

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A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
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Primer-Free Aptamer Selection Using A Random DNA Library
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Magnetically Detected Protein Binding Using Spin-Labeled Slow Off-Rate Modified Aptamers.

Shutian Lu1, Catherine R Fowler2, Brian Ream2

  • 1Department of Chemistry, University of Washington, Seattle, Washington 98195, United States.

ACS Sensors
|June 10, 2023
PubMed
Summary
This summary is machine-generated.

This study introduces a novel aptamer-based biosensor for protein detection. Immobilized modified aptamers (SOMAmers) with spin labels detect protein binding through changes in mobility, measurable by electron paramagnetic resonance (EPR) spectroscopy.

Keywords:
EPR spectroscopyaptamerprotein assayquantum sensingspin labeling

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Materials Science

Background:

  • Aptamer chemistry advancements enable new protein biosensing tools.
  • Slow off-rate modified aptamers (SOMAmers) offer high specificity for protein targets.
  • Site-specific labeling is crucial for precise molecular probes.

Purpose of the Study:

  • To develop and validate a novel protein biosensing platform using site-specifically labeled SOMAmers.
  • To investigate the detection of protein binding events via changes in spin label mobility.
  • To explore the integration of this system with diamond nitrogen-vacancy (NV) center relaxometry for enhanced detection.

Main Methods:

  • Immobilization of site-specifically nitroxide radical-labeled SOMAmers using azide-alkyne click chemistry.
  • Detection of protein binding by monitoring changes in spin label rotational mobility using electron paramagnetic resonance (EPR) spectroscopy.
  • Modeling the combined system with diamond nitrogen-vacancy (NV) center relaxometry.

Main Results:

  • Demonstrated workflow using SOMAmer SL5 and platelet-derived growth factor B (PDGF-BB).
  • Identified optimal labeling sites on SOMAmers exhibiting significant mobility changes upon protein binding.
  • Showcased the potential for NV center relaxometry to detect SOMAmer-protein interactions.

Conclusions:

  • The developed spin label-mediated assay provides a general method for detecting protein binding events.
  • This approach transduces molecular recognition into magnetically detectable signals.
  • The system holds promise for sensitive and specific protein biosensing applications.