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Related Concept Videos

Integrins01:10

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Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
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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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Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
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Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
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αvβ3- or α5β1-Integrin-Selective Peptidomimetics for Surface Coating.

Carlos Mas-Moruno1, Roberta Fraioli2, Florian Rechenmacher3

  • 1Biomaterials, Biomechanics and Tissue Engineering Group, Department of Materials Science and Metallurgical Engineering and Centre for Research in NanoEngineering, Universitat Politècnica de Catalunya (UPC), Diagonal 647, 08028, Barcelona, Spain. carles.mas.moruno@upc.edu.

Angewandte Chemie (International Ed. in English)
|June 4, 2016
PubMed
Summary

Researchers are developing advanced biomaterials that can bind to integrins, improving cell adhesion and guiding biological responses. This review highlights the shift from simple peptides to sophisticated peptidomimetics for precise control over cell behavior and tissue engineering applications.

Keywords:
RGD peptidesintegrinspeptidomimeticsreceptor selectivitysurface coating

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Area of Science:

  • Biomaterials Science
  • Cell Biology
  • Surface Chemistry

Background:

  • Biomaterials engineered with integrin-binding motifs enhance cell adhesion and biological responses.
  • Current approaches range from peptides and proteins to advanced peptidomimetics.

Purpose of the Study:

  • To review the evolution of surface-coating molecules for integrin binding.
  • To focus on the challenge of achieving selectivity between integrin subtypes αvβ3 and α5β1.
  • To explore the potential of peptidomimetics for creating cell-instructive surfaces.

Main Methods:

  • Review of scientific literature on biomaterial functionalization.
  • Analysis of peptide and peptidomimetic ligand development for integrin binding.
  • Discussion of surface modification strategies for enhanced selectivity.

Main Results:

  • Evolution from low-activity peptides to high-activity, selective peptidomimetic ligands.
  • Progress in designing ligands with specific binding to integrin subtypes.
  • Demonstration of peptidomimetics' potential for precise biological control.

Conclusions:

  • Peptidomimetic functionalization enables highly specific cell-instructive surfaces.
  • These surfaces are valuable for dissecting integrin subtype roles.
  • Applications in tissue engineering and regenerative medicine are advanced by this technology.