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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
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Oligosaccharide Assembly01:24

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Peptide Bonds02:43

Peptide Bonds

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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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Membrane Carbohydrates01:30

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The plasma membrane is a dynamic barrier composed of lipids, proteins, and carbohydrates. It is the epicenter of many cellular processes required for cell growth and survival. Carbohydrates have unique structural and chemical properties that help the plasma membrane to carry out its functions effectively.
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Proteoglycans01:05

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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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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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Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library
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Peptide mimotopes to emulate carbohydrates.

Teruhiko Matsubara1

  • 1Department of Biosciences and Informatics, Keio University, 3-14-1 Hiyoshi, Kouhoku-ku, Yokohama 223-8522, Japan. matsubara@bio.keio.ac.jp.

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Summary

Peptide mimotopes offer a promising alternative to complex glycans for understanding and treating glycan-related diseases. Phage-display technology efficiently identifies these mimotopes for therapeutic applications.

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Area of Science:

  • Glycobiology
  • Immunology
  • Biotechnology

Background:

  • Cell surface glycoconjugates play critical roles in biological processes and diseases, including cancer metastasis and infections.
  • Effective therapeutic strategies for glycan-related diseases require understanding and regulating glycan-protein interactions.
  • Synthesizing diverse glycan derivatives is challenging, necessitating alternative approaches.

Purpose of the Study:

  • To explore peptide mimotopes as alternatives to natural glycan ligands for therapeutic development.
  • To review the advantages, mimicry, and applications of glycan-mimetic peptides.
  • To provide insights into library design and affinity improvement for peptide mimotopes.

Main Methods:

  • Utilizing phage-display technology for the selection of glycan-mimetic peptide mimotopes from large libraries.
  • Comparing the efficacy and characteristics of peptide mimotopes versus natural glycan ligands.
  • Describing library design strategies and methods for enhancing peptide affinity.

Main Results:

  • Peptide mimotopes can effectively mimic natural glycans and are recognized by glycan-binding proteins.
  • Phage display is a powerful tool for identifying functional glycan-mimetic peptides.
  • Strategies for improving the affinity of peptide mimotopes have been developed.

Conclusions:

  • Glycan-mimetic peptides present a viable and advantageous alternative to complex glycans for research and therapy.
  • Phage display facilitates the discovery and optimization of these peptide-based therapeutics.
  • Peptide mimotopes hold significant potential for vaccine development against glycan-related targets.