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Peptide Bonds02:43

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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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Density, specific weight, specific gravity, and compressibility are fundamental properties of fluids. Density is the mass per unit volume, characterizing the mass of a fluid system. It influences buoyancy, pressure, flow dynamics, viscosity, thermal conductivity, and sound propagation. For instance, in pipeline design, accurate density measurements ensure that the pipeline can handle the fluid's mass.
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Peptide Identification Using Tandem Mass Spectrometry01:33

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Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
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Multicellular organisms contain a variety of structurally and functionally distinct cell types, but the DNA in all the cells originated from the same parent cells. The differences in the cells can be attributed to the differential gene expression. Liver cells, whose functions include detoxification of blood, production of bile to metabolize fats, and synthesis of proteins essential for metabolism, must express a specific set of genes to perform their functions. Gene expression also varies with...
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Related Experiment Video

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Analysis of Simian Immunodeficiency Virus-specific CD8+ T-cells in Rhesus Macaques by Peptide-MHC-I Tetramer Staining
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Specific MHC-I Peptides Are Induced Using PROTACs.

Stephanie M Jensen1, Gregory K Potts1, Damien B Ready1

  • 1Discovery Chemistry and Technology, AbbVie North Chicago, IL, United States.

Frontiers in Immunology
|December 8, 2018
PubMed
Summary
This summary is machine-generated.

Proteolysis targeting chimera (PROTAC) compounds can induce the presentation of specific MHC class-I peptides from endogenous proteins. This discovery offers new avenues for developing T-cell-based immunotherapies and identifying novel therapeutic targets.

Keywords:
BETHLAMHC-IPROTACimmunopeptides

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Area of Science:

  • Immunology
  • Proteomics
  • Drug Discovery

Background:

  • Major histocompatibility complex class-I (MHC-I) presented peptides are crucial for immunotherapy.
  • Identifying these peptide targets is key for developing T-cell-based therapeutics.

Purpose of the Study:

  • To investigate the potential of proteolysis targeting chimera (PROTAC) compounds to induce the presentation of endogenous MHC-I peptides.
  • To explore the relationship between PROTAC treatment, protein degradation, and peptide presentation.
  • To analyze PROTAC-induced changes in the immunopeptidome for novel immunotherapy targets.

Main Methods:

  • Utilized liquid chromatography-tandem mass spectrometry (LC-MS/MS) to identify MHC-I peptides.
  • Employed label-free mass spectrometry quantification to measure peptide presentation rates.
  • Analyzed the global immunopeptidome following PROTAC treatment.

Main Results:

  • Identified BET-derived MHC-I peptides induced by BET-directed PROTAC compounds.
  • Demonstrated a direct correlation between the rate of protein degradation and the rate of peptide presentation.
  • Discovered numerous new peptides presented in a PROTAC-specific manner, mapping to the BET pathway and other potential pathways.

Conclusions:

  • PROTAC compounds can effectively induce the presentation of MHC-I peptides from endogenous proteins.
  • This mechanism provides a novel strategy for discovering and generating new immunotherapy targets.
  • Highlights the potential of PROTACs in advancing T-cell-based therapeutic development.