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Related Concept Videos

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...
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...
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...

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Related Experiment Video

Updated: Jun 8, 2026

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

Functionalizable collagen model peptides.

Roman S Erdmann1, Helma Wennemers

  • 1Department of Chemistry, University of Basel, St. Johanns-Ring 19, 4056 Basel, Switzerland.

Journal of the American Chemical Society
|September 21, 2010
PubMed
Summary
This summary is machine-generated.

Azidoproline (Azp) stabilizes collagen triple helices similarly to hydroxyproline. Click chemistry allows easy functionalization of these peptides, creating novel collagen-based materials.

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Published on: February 7, 2018

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Last Updated: Jun 8, 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

Published on: January 31, 2014

Recombinant Collagen I Peptide Microcarriers for Cell Expansion and Their Potential Use As Cell Delivery System in a Bioreactor Model
08:43

Recombinant Collagen I Peptide Microcarriers for Cell Expansion and Their Potential Use As Cell Delivery System in a Bioreactor Model

Published on: February 7, 2018

Area of Science:

  • Biochemistry
  • Materials Science
  • Peptide Chemistry

Background:

  • Collagen is a crucial structural protein.
  • Modifying collagen peptides enhances their properties.
  • Azidoproline (Azp) is a proline analog.

Purpose of the Study:

  • Investigate the conformational properties of azidoproline-containing collagen model peptides (CMPs).
  • Assess the collagen triple helix stabilizing effect of (4R)Azp.
  • Explore the functionalizability of Azp-containing CMPs via click chemistry.

Main Methods:

  • Synthesis of azidoproline-containing collagen model peptides.
  • Analysis of peptide conformational properties.
  • Application of click chemistry for peptide functionalization.

Main Results:

  • (4R)Azp demonstrated a collagen triple helix stabilizing effect comparable to (4R)hydroxyproline.
  • Azp-containing CMPs were readily functionalized using click chemistry.
  • Triazole-functionalized CMPs formed stable triple helices, tolerating sterically demanding moieties.

Conclusions:

  • Azidoproline is a viable proline analog for stabilizing collagen triple helices.
  • Click chemistry provides a facile route for functionalizing Azp-containing collagen peptides.
  • These findings suggest potential for developing advanced functional collagen-based materials.