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Related Concept Videos

Fibronectins Connect Cells with ECM01:25

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Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
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The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...
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In animal cells, the extracellular matrix allows cells within tissues to withstand external stresses and transmits signals from the outside of the cell to the inside. The extracellular matrix is extensive, and its composition varies between different types of tissues. For example, the reticular fibers and ground substance make up the ECM in loose connective tissue, while collagen and bone minerals make up the ECM of bone tissue. 
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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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The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
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Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
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Updated: Jan 8, 2026

ECM Protein Nanofibers and Nanostructures Engineered Using Surface-initiated Assembly
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A novel fibronectin-binding peptide reveals dynamic intermediate structures during matrix assembly.

Henry A Resnikoff1, Aaron J Hamlin1, Faith M Reash1

  • 1Department of Molecular Biology, Princeton University, Princeton, NJ, 08544-1014, USA.

Scientific Reports
|December 23, 2025
PubMed
Summary

Researchers identified a fibronectin-binding peptide (S2) that targets fibronectin fibrils. This peptide enables visualization of extracellular matrix assembly and can be used to develop new tools for studying the matrix.

Keywords:
Extracellular matrixFibronectinGFP fusion proteinLive-imagingMatrix assemblyPhage display

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Biomaterials Science

Background:

  • The extracellular matrix (ECM) is crucial for cell functions and tissue development.
  • Dysregulation of the ECM, particularly fibronectin (FN), is linked to fibrotic diseases.
  • Understanding FN assembly is key to developing new therapeutic strategies.

Purpose of the Study:

  • To identify novel fibronectin-binding peptides for studying ECM assembly.
  • To develop tools for real-time visualization and analysis of fibronectin fibril formation.

Main Methods:

  • M13 phage display was used to isolate fibronectin-binding peptides.
  • A fusion protein (GST-S2-EGFP) was engineered to incorporate the S2 peptide.
  • Live cell imaging and analysis of decellularized matrices were performed.

Main Results:

  • The S2 peptide specifically binds to fibronectin and directs fusion proteins into FN fibrils.
  • GST-S2-EGFP allows real-time visualization of fibronectin matrix assembly, including nucleation and elongation.
  • The S2 fusion protein demonstrates stable association with fibronectin in decellularized matrices.

Conclusions:

  • The S2 peptide is a valuable tool for dissecting fibronectin assembly dynamics.
  • This approach enables the generation of fluorescent scaffolds for ECM research.
  • The S2 peptide can direct functional proteins to the fibronectin matrix for therapeutic applications.