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Related Concept Videos

Complexation Equilibria: The Chelate Effect01:19

Complexation Equilibria: The Chelate Effect

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In complexation reactions, metal atoms or cations interact with ligands to form donor-acceptor adducts called metal complexes. Ligands that bind through one donor site are monodentate, ligands with two donor sites are bidentate, and those with more than two donor sites are polydentate ligands. For example, ethylene diamine is a bidentate ligand that binds through two nitrogen donor atoms, forming a five-membered ring. EDTA is a polydentate ligand that binds through four oxygen and two nitrogen...
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Different monodentate and polydentate ligands are used as complexing agents in complexometric titration reactions. The formation of complexes by mono- and bidentate ligands involves two or more intermediate steps, limiting their use as complexing agents. In comparison, polydentate ligands can form complexes with metal ions in a single-step process, facilitating sharper end points. This means polydentate ligands, such as amino carboxylic acid derivatives, are most commonly employed in...
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EDTA: Chemistry and Properties01:22

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Polydentate ligands are most widely used in complexometric titrations because they form more stable complexes with the metal ions than mono- or bidentate ligands due to the chelate effect. Examples of polydentate ligands are ethylenediaminetetraacetic acid (EDTA), crown ethers, and cryptands. The most important feature of optimal polydentate ligands is the ability to form 1:1 complexes in a single-step process. Amino carboxylic acid derivatives are frequently used as complexing agents. EDTA is...
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The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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EDTA titrations may necessitate masking and demasking agents to temporarily protect a particular metal ion in a mixture from the EDTA reaction. These agents facilitate the sequential analysis of the metal ions by forming stable complexes with some—but not all—metal ions during certain steps.
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Multivalent chelators for spatially and temporally controlled protein functionalization.

Changjiang You1, Jacob Piehler

  • 1Department of Biology, University of Osnabrück, Barbarastr. 11, 49076, Osnabrück, Germany.

Analytical and Bioanalytical Chemistry
|April 29, 2014
PubMed
Summary

Multivalent chelators (MCH) offer efficient, reversible protein modification using oligohistidine (His)-tags. This technology enables advanced bioanalytical applications, including protein interaction analysis and cell labeling.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Bioanalytical Chemistry

Background:

  • Site-specific protein modification is crucial for bioanalytical applications like immobilization and labeling.
  • Existing methods using peptide tags often lack efficiency and bio-orthogonality.

Purpose of the Study:

  • To review the application of multivalent chelators (MCH) for high-affinity, reversible recognition of oligohistidine (His)-tagged proteins.
  • To highlight the versatility of MCH in handling and modifying recombinant proteins for bioanalytical purposes.

Main Methods:

  • Utilizing multivalent chelators (MCH) composed of multiple nitrilotriacetic acid (NTA) moieties on molecular scaffolds.
  • Employing transition metal ions to mediate reversible interactions between MCH and His-tagged proteins.
  • Conjugating MCH to surfaces, probes, or other biomolecules for various applications.

Main Results:

  • MCH provide sub-nanomolar binding affinity for His-tagged proteins with rapid dissociation capabilities.
  • The small size and biochemical compatibility of MCH ensure versatile protein handling.
  • Demonstrated applications in quantitative protein interaction analysis on patterned surfaces and specific protein labeling in living cells.

Conclusions:

  • MCH represent a powerful tool for efficient and bio-orthogonal protein modification and handling.
  • The reversible nature and high affinity of MCH-His-tag interactions enable diverse bioanalytical strategies.
  • This technology facilitates advanced applications in protein interaction studies and cellular labeling.