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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...
Fibrous Proteins00:55

Fibrous Proteins

Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
Collagens are the Major Structural Proteins of ECM01:13

Collagens are the Major Structural Proteins of ECM

Three main types of fibers are secreted by fibroblasts: collagen fibers, elastic fibers, and reticular fibers. Collagen fiber is made from fibrous protein subunits linked together to form a long, straight fiber. Collagen fibers, while flexible, have great tensile strength, resist stretching, and give ligaments and tendons their characteristic resilience and strength. These fibers hold connective tissues together, even during the body's movement.
Connective tissue proper includes loose...
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...
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...
Clot Retraction and Fibrinolysis01:16

Clot Retraction and Fibrinolysis

After a fibrin clot is formed, the next step is clot retraction, a vital process facilitated by platelet contractile proteins, such as actin and myosin. These proteins pull the fibrin strands closer together and condense the clot. This action reduces the size of the clot, creating a smaller, denser structure that effectively seals off the damaged vessel. Clot retraction consolidates the clot and helps with wound healing by bringing the edges of the damaged blood vessel closer together.

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Related Experiment Video

Updated: Jul 7, 2026

Production of Nanofibrillar Patterned Collagen for Tissue Engineering
07:34

Production of Nanofibrillar Patterned Collagen for Tissue Engineering

Published on: September 20, 2024

Fibrillogenesis in dense collagen solutions: a physicochemical study.

F Gobeaux1, G Mosser, A Anglo

  • 1Chimie de la Matière Condensée, UMR 7574 CNRS-Université Pierre et Marie Curie, ENSCP-Ecole Pratique des Hautes Etudes, 12 rue Cuvier, 75005 Paris, France.

Journal of Molecular Biology
|February 1, 2008
PubMed
Summary

Collagen fibrillogenesis in vitro is governed by concentration, pH, and ionic strength, forming strong gels similar to connective tissues. These physicochemical factors dictate collagen

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In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen

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Last Updated: Jul 7, 2026

Production of Nanofibrillar Patterned Collagen for Tissue Engineering
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Published on: September 20, 2024

Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo
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In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
07:54

In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen

Published on: September 20, 2012

Area of Science:

  • Biochemistry
  • Materials Science
  • Biophysics

Background:

  • Fibrillogenesis, the process of collagen fibril formation, is crucial for connective tissue development.
  • Understanding cellular influence on fibrillogenesis requires studying collagen self-assembly under physiological conditions.

Purpose of the Study:

  • To investigate the physicochemical parameters influencing type I collagen self-assembly into fibrils in vitro.
  • To model fibrillogenesis at collagen concentrations mimicking those found in living tissues.

Main Methods:

  • Systematic study of type I collagen self-assembly in solutions (40-300 mg/ml).
  • Utilized transmission electron microscopy (TEM) and small- and wide-angle X-ray scattering (SAXS/WAXS).
  • Evaluated effects of collagen concentration, pH (2.5-12), and ionic strength (24-261 mM) on fibril formation and gel structure.

Main Results:

  • High collagen concentrations (40-300 mg/ml) formed strong gels across wide pH and ionic strength ranges.
  • Consistent cross-striated collagen fibril patterns and 67-nm long spacing (SAXS) observed from pH 6 to 12.
  • Collagen concentration significantly impacted gel structure and fibril morphology; increasing ionic strength led to larger fibrils.

Conclusions:

  • Physicochemical parameters like concentration, pH, and ionic strength precisely control collagen molecular organization and fibrillogenesis.
  • The in vitro model replicates in vivo conditions, enabling detailed study of collagen self-assembly in tissue morphogenesis.