Related Experiment Video
Updated: Apr 23, 2026
07:34
Production of Nanofibrillar Patterned Collagen for Tissue Engineering
Published on: September 20, 2024
1.2K
Understanding and controlling type I collagen adsorption and assembly at interfaces, and application to cell
1Université catholique de Louvain, Institute of Condensed Matter and Nanosciences, Croix du Sud 1 (L7.04.01), 1348 Louvain-la-Neuve, Belgium.
Colloids and Surfaces. B, Biointerfaces
|September 24, 2014
Summary
Controlling collagen adsorption and assembly at interfaces is key for biomaterials and tissue engineering. This review details methods to manipulate collagen organization, influencing cell behavior for advanced biointerfaces.
Area of Science:
- Biomaterials Science
- Tissue Engineering
- Protein Adsorption
- Extracellular Matrix
Background:
- Collagen is a major anisotropic, self-assembling protein in the extracellular matrix.
- Understanding collagen adsorption and assembly at interfaces is crucial for developing novel biointerfaces.
- This review summarizes twenty years of research on type I collagen adsorption and its control.
Purpose of the Study:
- To review methods for controlling collagen adsorption and assembly at interfaces.
- To explore how substrate properties and adsorption conditions influence collagen organization.
- To demonstrate the impact of controlled collagen organization on cell behavior for biomaterials applications.
Main Methods:
- Investigating the effects of substrate chemical nature and adsorption conditions (concentration, duration) on collagen adsorption.
- Designing substrates for spatial control of collagen adsorption using chemically heterogeneous surfaces.
- Employing mixed polymer brushes for temporal control of collagen adsorption and desorption via pH and ionic strength.
- Fabricating collagen-based nanotubes using layer-by-layer assembly in nanoporous templates and electrophoretic deposition.
Main Results:
- Substrate chemistry and adsorption conditions significantly affect collagen adsorption amount and supramolecular organization.
- Hydrophobic substrates and high adsorbed amounts promote collagen assembly.
- Chemically heterogeneous substrates with controlled domain sizes influence collagen assembly.
- Reversible adsorption/desorption of collagen was achieved using mixed polymer brushes.
- Collagen nanotubes were successfully fabricated and deposited onto substrates.
- Controlled collagen organization on biointerfaces demonstrably alters cell behavior.
Conclusions:
- The chemical nature and adsorption conditions critically influence collagen adsorption and assembly at interfaces.
- Tailored substrate design and stimuli-responsive materials enable precise control over collagen organization.
- Controlled collagen supramolecular organization is a viable strategy for engineering biointerfaces that modulate cell behavior, with applications in biomaterials science and tissue engineering.
Related Concept Videos
01:56Structural Protein Function
28.8K
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...
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...
28.8K
01:11Fibril-associated Collagen
2.7K
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...
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...
2.7K
01:24Overview of Cell-Matrix Interactions
7.9K
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...
7.9K
01:13Cell-matrix's Response to Mechanical Forces
2.7K
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...
Anchoring junctions mechanically attach a cell to the...
2.7K
01:05Type IV Collagen of Basal Lamina
2.5K
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...
A type IV collagen molecule has six alpha chains which can...
2.5K
01:10Integrins
4.8K
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.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
4.8K