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Related Concept Videos

Selectins01:25

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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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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.
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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Related Experiment Video

Updated: Sep 23, 2025

Production of Elastin-like Protein Hydrogels for Encapsulation and Immunostaining of Cells in 3D
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Multivalent Elastin-Like Glycopolypeptides: Subtle Chemical Structure Modifications with High Impact on Lectin

Marie Rosselin1, Zoeisha S Chinoy1, Lourdes Mónica Bravo-Anaya1

  • 1Université de Bordeaux, CNRS, Bordeaux INP, LCPO, UMR 5629, Pessac F-33600, France.

ACS Macro Letters
|May 13, 2022
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Summary

Synthetic glycopolypeptides were studied for lectin binding. Key factors for binding to RCA120 include a galactose linker and no positive charge on the sugar-holding residue.

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A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
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Area of Science:

  • Biochemistry
  • Polymer Science
  • Glycobiology

Background:

  • Elastin-like polypeptides (ELPs) are versatile biomaterials.
  • Glycopolypeptides combine polypeptide properties with carbohydrate recognition.
  • Lectin binding is crucial for cellular interactions and drug delivery.

Purpose of the Study:

  • To synthesize and screen a library of synthetic elastin-like glycopolypeptides.
  • To identify structural parameters influencing lectin binding efficacy.
  • To understand the molecular basis of RCA120 binding to glycopolypeptides.

Main Methods:

  • Synthesis of a library of elastin-like glycopolypeptides with varying structures.
  • Screening of glycopolypeptides using microscale thermophoresis.
  • Analysis of structural features such as polypeptide backbone size, glycovalency, linker presence, and charge.

Main Results:

  • Polypeptide backbone size and glycovalency showed minimal impact on lectin binding.
  • The presence of a linker at the anomeric position of galactose was critical for binding.
  • Absence of positive charge on the polypeptide residue holding the sugar unit was essential for RCA120 binding.

Conclusions:

  • Specific structural features, not overall size or sugar density, dictate lectin binding.
  • Anomeric linkage and charge neutralization are key design principles for targeted lectin interactions.
  • These findings inform the rational design of glycopolypeptides for applications in diagnostics and therapeutics.