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Fibril-associated Collagen

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...

Collagens are the Major Structural Proteins of ECM

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.
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Type IV Collagen of Basal Lamina

Type IV Collagen of Basal Lamina

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Structural Protein Function

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Related Experiment Video

Updated: Jul 19, 2026

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

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

Published on: January 31, 2014

Macrocyclic scaffold for the collagen triple helix.

Jia-Cherng Horng¹, Andrew J Hawk, Qian Zhao

¹Departments of Biochemistry and Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.

Organic Letters

|October 6, 2006

Summary

Researchers created a synthetic collagen using a macrocyclic scaffold. This scaffold enhances collagen triple helix stability and allows concentration-independent folding, advancing synthetic collagen applications.

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Production of Nanofibrillar Patterned Collagen for Tissue Engineering

Production of Nanofibrillar Patterned Collagen for Tissue Engineering

Published on: September 20, 2024

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Last Updated: Jul 19, 2026

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

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

Published on: January 31, 2014

Production of Nanofibrillar Patterned Collagen for Tissue Engineering

Production of Nanofibrillar Patterned Collagen for Tissue Engineering

Published on: September 20, 2024

Area of Science:

Biochemistry
Materials Science
Polymer Chemistry

Background:

Natural collagen's triple helix structure is crucial for its function.
Covalent cross-linking is a known method to stabilize collagen structures.
Understanding collagen self-assembly is key to biomaterial development.

Purpose of the Study:

To design and synthesize a novel collagen mimetic.
To investigate the impact of a rigid scaffold on collagen triple helix formation and stability.
To develop a concentration-independent folding system for synthetic collagens.

Main Methods:

Synthesis of a C(3)-symmetric macrocyclic scaffold.
Attachment of collagen peptide strands to the scaffold.
Structural analysis of the resulting synthetic collagen complex.
Assessment of folding behavior and conformational stability.

Main Results:

Successful synthesis of a synthetic collagen with strands pendent on a macrocyclic scaffold.
The scaffold induced conformational stability in the collagen triple helix.
Folding of the synthetic collagen was independent of concentration.
Demonstrated the potential for controlled collagen self-assembly.

Conclusions:

A novel synthetic collagen with enhanced stability and predictable folding has been developed.
The macrocyclic scaffold is an effective strategy for controlling collagen structure and function.
This work provides a foundation for the design of advanced collagen-based biomaterials.