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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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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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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.
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Analyzing Dynamic Protein Complexes Assembled On and Released From Biolayer Interferometry Biosensor Using Mass Spectrometry and Electron Microscopy
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Saccharide-Containing Dynamic Proteoids.

Yun Liu1, Marc C A Stuart1,2, Martin D Witte1

  • 1Stratingh Institute for Chemistry, University of Groningen, Nijenborgh 7, 9747 AG, Groningen, The Netherlands.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|October 6, 2017
PubMed
Summary
This summary is machine-generated.

Researchers created novel sugar-containing dynamic proteoid biodynamers for adaptive biomaterials. These compounds utilize saccharide-based dialdehydes to improve biocompatibility, offering enhanced material properties.

Keywords:
biodynamersdynamic proteoidsequilibrium polymerizationnanostructuressupramolecular chemistry

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Area of Science:

  • Biomaterials Science
  • Polymer Chemistry
  • Organic Synthesis

Background:

  • Dynamic proteoids are adaptive biomaterials with dynamic covalent bonds, mimicking protein structures.
  • Existing biodynamers lack enhanced biocompatibility for advanced applications.

Purpose of the Study:

  • To design and synthesize novel sugar-containing dynamic proteoid biodynamers.
  • To enhance the biocompatibility of biodynamers using saccharide-based components.

Main Methods:

  • Polycondensation reactions involving amino acid/dipeptide hydrazides and dialdehydes (biological aliphatic and nonbiological aromatic).
  • Incorporation of saccharide-based dialdehydes into the biodynamer structure.

Main Results:

  • Successful synthesis of a range of sugar-containing dynamic proteoid biodynamers.
  • Demonstrated potential for enhanced biocompatibility due to saccharide integration.

Conclusions:

  • Sugar-containing dynamic proteoid biodynamers represent a promising class of adaptive biomaterials.
  • The use of saccharide-based dialdehydes is a viable strategy for improving biodynamer biocompatibility.