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Related Concept Videos

Affinity Chromatography01:03

Affinity Chromatography

Affinity chromatography is a powerful technique extensively utilized for separating and purifying specific biomolecules from complex mixtures. It capitalizes on the highly selective binding between an analyte and its counterpart, such as antibody-antigen interactions. The counterpart is immobilized on the stationary phase, forming an affinity column. The stationary phase typically consists of solid support, such as agarose or porous glass beads, immobilizing the affinity ligand. The mobile...
Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...
Labeling DNA Probes03:31

Labeling DNA Probes

DNA probes are fragments of DNA labeled with a reporter tag to enable their detection or purification. The resulting labeled DNA probes can then hybridize to target nucleic acid sequences through complementary base-pairing, and may be used to recover or identify these regions.
Radioisotopes, fluorophores, or small molecule binding partners like biotin or digoxigenin, are the most widely used reporter tags for labeling DNA probes. These labels can be attached to the probe DNA molecule via...
Affinity and Avidity01:41

Affinity and Avidity

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Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
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Aptamer-based affinity labeling of proteins.

Jan L Vinkenborg1, Günter Mayer, Michael Famulok

  • 1University of Bonn, LIMES Institute, Bonn, Germany.

Angewandte Chemie (International Ed. in English)
|August 7, 2012
PubMed
Summary

A new method called aptamer-based affinity labeling (ABAL) allows labeled aptamers to bind targets with light-activated specificity. This technique enables enrichment of aptamer-protein complexes from cells for studying interactions.

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Identification of Small Molecule-binding Proteins in a Native Cellular Environment by Live-cell Photoaffinity Labeling

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Chemical Biology

Background:

  • Aptamers are nucleic acid-based ligands with high specificity for target molecules.
  • Studying aptamer-target interactions within complex biological systems remains challenging.

Purpose of the Study:

  • To develop a novel method for labeling and enriching aptamer-protein complexes.
  • To enable the study of aptamer interactions in native cellular environments.

Main Methods:

  • Development of aptamer-based affinity labeling (ABAL) strategy.
  • Utilizing light-dependent cross-linking of labeled aptamers to target proteins.
  • Enrichment of aptamer-protein complexes from cellular lysates and surfaces of living cells.

Main Results:

  • Demonstrated highly specific and light-dependent cross-linking of aptamers to their protein targets.
  • Successfully enriched aptamer-protein complexes from both in vitro and in vivo cellular contexts.
  • Established a new tool for investigating aptamer-protein interactions.

Conclusions:

  • Aptamer-based affinity labeling (ABAL) provides a powerful and specific method for identifying and studying aptamer-target interactions.
  • This technique facilitates the analysis of aptamer binding in complex biological samples, including living cells.
  • ABAL opens new avenues for proteomic research and drug discovery using aptamers.