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Related Concept Videos

Ligand Binding Sites02:40

Ligand Binding Sites

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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
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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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Complexometric Titration: Ligands00:43

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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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Labeling DNA Probes03:31

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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.
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Conserved Binding Sites01:49

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
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DNA-Encoded Library Technology─A Catalyst for Covalent Ligand Discovery.

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|March 25, 2024
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Summary

Novel covalent ligands for drug discovery are increasingly identified using DNA-encoded library (DEL) technology. While chemoproteomics aids in characterizing these molecules, further advancements are needed to fully leverage DEL for covalent ligand discovery.

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Area of Science:

  • Medicinal Chemistry
  • Chemical Biology
  • Drug Discovery

Background:

  • Historically, identifying novel covalent ligands relied on serendipity, with dedicated techniques emerging in the early 2000s.
  • Chemoproteomics advances enable robust characterization of covalent drugs, mitigating associated liabilities and renewing interest in this modality.
  • DNA-encoded library (DEL) technology has become a powerful tool for identifying novel chemical matter against protein targets.

Purpose of the Study:

  • To explore current approaches in covalent DNA-encoded library (DEL) technology.
  • To reflect on the future directions and advancements needed to fully realize the potential of DEL for covalent ligand discovery.

Main Methods:

  • Review of existing literature and methodologies in covalent DEL synthesis.
  • Analysis of chemoproteomic approaches for characterizing covalent hit molecules.
  • Discussion of challenges and opportunities in covalent DEL hit identification.

Main Results:

  • Several commercial and academic groups have reported methods for covalent DEL synthesis and hit identification.
  • Despite progress, significant potential remains untapped in applying DEL technology for covalent ligand discovery.
  • Chemoproteomics plays a crucial role in derisking covalent hit molecules.

Conclusions:

  • Covalent ligand discovery using DEL technology is a rapidly advancing field with significant therapeutic potential.
  • Further innovation in covalent DEL synthesis and screening methodologies is required.
  • Integrating chemoproteomics is essential for successful covalent drug development.