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Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...
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The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
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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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A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
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Block-Sequence-Specific Glycopolypeptides with Selective Lectin Binding Properties.

Cristina Lavilla1, Gokhan Yilmaz2, Veselina Uzunova3

  • 1Department of Chemical Engineering and Chemistry, Eindhoven University of Technology , Den Dolech 2, 5612AZ Eindhoven, The Netherlands.

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Summary

Synthetic glycopolypeptides with controlled structures selectively bind to different lectins. This research highlights the importance of precise carbohydrate arrangement in glycopeptides for specific biological interactions.

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Area of Science:

  • Polymer Chemistry
  • Glycobiology
  • Biomaterials Science

Background:

  • Glycopolypeptides are crucial in biological recognition.
  • Controlling carbohydrate presentation in synthetic polymers is challenging.
  • Understanding structure-activity relationships is key for targeted applications.

Purpose of the Study:

  • To synthesize glycopolypeptides with defined block sequences.
  • To investigate the impact of sequence and block length on secondary structure.
  • To evaluate lectin binding specificity based on glycopolypeptide architecture.

Main Methods:

  • Sequential N-carboxyanhydride (NCA) polymerization.
  • Selective deprotection and functionalization.
  • Circular dichroism (CD) spectroscopy for secondary structure analysis.
  • Turbidity measurements and surface plasmon resonance (SPR) for lectin binding studies.

Main Results:

  • Glycopolypeptides with varied galactose unit arrangements and block lengths were successfully synthesized.
  • Secondary structure varied with composition; octablock structures were α-helical, others were random coils.
  • Lectin binding affinity and specificity were dependent on glycopolypeptide structure.
  • Octablock and tetrablock glycopolypeptides showed distinct preferences for RCA120 and Galectin-3, respectively.

Conclusions:

  • Precise control over carbohydrate presentation in synthetic glycopolypeptides influences secondary structure and lectin interactions.
  • Different lectins exhibit sensitivity to specific glyco-coding patterns.
  • Tailoring glycopeptide architecture is vital for developing targeted biomaterials and understanding biological recognition.