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Related Concept Videos

Fibril-associated Collagen01:11

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
Cell-matrix's Response to Mechanical Forces01:13

Cell-matrix's Response to Mechanical Forces

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. 
Anchoring junctions mechanically attach a cell to the...
Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

Type IV collagen is a 400 nm long, network-forming collagen that acts as a barrier between the epithelial and endothelial cells. Type IV collagen  forms the backbone of the basement membrane by scaffolding with laminin, entactin, proteoglycans, and fibronectin. Apart from rendering structural support to the basement membrane, it also helps entail signaling potentials necessary for both pathological and physiological functions.
A type IV collagen molecule has six alpha chains which can exist in...
Structural Protein Function01:56

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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 the...
Fibronectins Connect Cells with ECM01:25

Fibronectins Connect Cells with ECM

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.
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...

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Related Experiment Video

Updated: May 11, 2026

Multiplexed Single-molecule Force Proteolysis Measurements Using Magnetic Tweezers
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Multiplexed Single-molecule Force Proteolysis Measurements Using Magnetic Tweezers

Published on: July 25, 2012

Single-molecule level binding force between collagen and collagen binding domain-growth factor conjugates.

Xun Huang1, Xiaoran Li, Qiangbin Wang

  • 1i-LAB, Suzhou Institute of Nano-Tech and Nano-Bionics, Chinese Academy of Sciences, Suzhou, Jiangsu 215123, China.

Biomaterials
|May 28, 2013
PubMed
Summary

Collagen-binding domain (CBD) binding sites on collagen scaffolds are not uniform, influencing controlled growth factor release for tissue engineering. Understanding this interaction is key for regenerative medicine applications.

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Last Updated: May 11, 2026

Multiplexed Single-molecule Force Proteolysis Measurements Using Magnetic Tweezers
10:08

Multiplexed Single-molecule Force Proteolysis Measurements Using Magnetic Tweezers

Published on: July 25, 2012

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
07:03

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Published on: January 31, 2014

Area of Science:

  • Biomaterials Science
  • Tissue Engineering
  • Biophysics

Background:

  • Collagen/collagen binding domain (CBD)-growth factor composites show promise in tissue engineering and regeneration.
  • Fundamental biophysical questions regarding CBD binding and growth factor release mechanisms remain largely unaddressed.

Purpose of the Study:

  • To investigate the distribution of CBD binding sites on collagen scaffolds at the single-molecule level.
  • To elucidate the mechanism of controlled growth factor release from collagen scaffolds.

Main Methods:

  • Utilized atomic force spectroscopy (AFM)-based investigations.
  • Employed a quantum dot-based bimodal imaging method for visualization.
  • Conducted AFM force spectroscopy unbinding experiments.

Main Results:

  • Directly visualized non-uniformly distributed CBD binding sites on collagen membranes.
  • Revealed modest unbinding force and dissociation constant for the CBD/collagen interaction.

Conclusions:

  • The non-uniform distribution of CBD binding sites is a critical factor in controlled growth factor release.
  • The specific unbinding force and dissociation constant of the CBD/collagen interaction are crucial for successful controlled release applications in regenerative medicine.