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Fibril-associated Collagen01:11

Fibril-associated Collagen

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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...
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Collagens are the Major Structural Proteins of ECM01:13

Collagens are the Major Structural Proteins of ECM

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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...
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Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

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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...
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Structural Protein Function01:56

Structural Protein Function

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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...
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Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

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Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
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Cell-matrix's Response to Mechanical Forces01:13

Cell-matrix's Response to Mechanical Forces

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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. 
Anchoring junctions mechanically attach a cell to the...
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Related Experiment Video

Updated: Mar 10, 2026

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

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Intact Telopeptides Enhance Interactions between Collagens.

Marjan Shayegan1, Tuba Altindal2, Evan Kiefl3

  • 1Department of Chemistry, Simon Fraser University, Burnaby, Canada.

Biophysical Journal
|December 8, 2016
PubMed
Summary

Intact collagen telopeptides significantly enhance the viscoelasticity of collagen solutions. These findings suggest telopeptides mediate transient interactions crucial for collagen self-assembly and tissue function.

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

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Area of Science:

  • Biophysics
  • Materials Science
  • Biochemistry

Background:

  • Collagen is a primary structural protein in connective tissues and the extracellular matrix.
  • Collagen self-assembly into fibrils is vital for tissue development, homeostasis, and wound healing.
  • Telopeptides, nonhelical regions flanking the collagen triple helix, are known to influence assembly kinetics.

Purpose of the Study:

  • To investigate the role of intact telopeptides in collagen viscoelasticity.
  • To quantify the impact of telopeptides on collagen self-assembly dynamics.
  • To elucidate the mechanism by which telopeptides affect collagen interactions.

Main Methods:

  • Microrheology measurements using optical tweezers were employed.
  • Viscoelastic properties of collagen solutions with and without telopeptides were analyzed.
  • An analytical polymer association model was used for theoretical validation.

Main Results:

  • Intact telopeptides significantly enhance the frequency-dependent complex shear modulus of collagen solutions.
  • Experimental data align with an analytical model predicting polymer association.
  • A concentration-dependent crossover in G″/c was observed around 300 Hz.

Conclusions:

  • Telopeptides play a crucial role in modulating collagen's viscoelastic properties.
  • Telopeptides likely facilitate transient intermolecular interactions between collagen molecules.
  • These interactions are important for collagen self-assembly, even under acidic conditions.