Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

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...
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...
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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

A tribute to Dr. Serge N. Timasheff, our mentor.

Biophysical reviews·2021
Same author

Sustained release silk fibroin discs: Antibody and protein delivery for HIV prevention.

Journal of controlled release : official journal of the Controlled Release Society·2019
Same author

Subvisible (2-100 μm) particle analysis during biotherapeutic drug product development: Part 2, experience with the application of subvisible particle analysis.

Biologicals : journal of the International Association of Biological Standardization·2015
Same author

Subvisible (2-100 μm) Particle Analysis During Biotherapeutic Drug Product Development: Part 1, Considerations and Strategy.

Journal of pharmaceutical sciences·2015
Same author

Silk Nanofiber Hydrogels with Tunable Modulus to Regulate Nerve Stem Cell Fate.

Journal of materials chemistry. B·2014
Same author

High Throughput Screening of Dynamic Silk-Elastin-Like Protein Biomaterials.

Advanced functional materials·2014

Related Experiment Video

Updated: Jul 6, 2026

Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo
10:24

Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo

Published on: May 9, 2016

Guide to collagen characterization for biomaterial studies.

Leah C Abraham1, Erin Zuena, Bernardo Perez-Ramirez

  • 1Departments of Chemical and Biological Engineering, Tufts University, Medford, Massachusetts 02155, USA.

Journal of Biomedical Materials Research. Part B, Applied Biomaterials
|April 5, 2008
PubMed
Summary

Characterizing collagen structure, chemistry, and morphology is crucial for understanding its role in disease, healing, and biomaterial applications. Comprehensive analysis ensures reliable correlation between collagen properties and biological outcomes.

More Related Videos

An Improved Method for the Preparation of Type I Collagen From Skin
05:17

An Improved Method for the Preparation of Type I Collagen From Skin

Published on: January 21, 2014

Related Experiment Videos

Last Updated: Jul 6, 2026

Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo
10:24

Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo

Published on: May 9, 2016

An Improved Method for the Preparation of Type I Collagen From Skin
05:17

An Improved Method for the Preparation of Type I Collagen From Skin

Published on: January 21, 2014

Area of Science:

  • Biomaterials Science
  • Tissue Engineering
  • Biomedical Engineering

Background:

  • Collagen structure and remodeling are vital in disease pathology, healing, and tissue development.
  • Collagen matrices are extensively used in biomaterials and biomedical applications, influencing cellular behavior and tissue formation.
  • Collagen matrix structure impacts cellular aging and differentiation potential.

Purpose of the Study:

  • To emphasize the necessity of standardized analytical tools for characterizing commercial collagens.
  • To guide the comparative analysis of collagen properties for biological studies.
  • To correlate collagen biophysical and chemical features with biological outcomes.

Main Methods:

  • Characterization of structural properties: molecular mass, purity, helical content, thermal properties.
  • Analysis of chemical features: surface elemental analysis, hydrophobicity.
  • Assessment of morphological features at various length scales.

Main Results:

  • Analytical techniques applied to collagen biomaterial matrices are reviewed.
  • Case study on collagen remodeling by fibroblasts highlights the importance of characterization.
  • Demonstrated the critical need for understanding collagen biophysical and chemical properties.

Conclusions:

  • Comprehensive characterization of collagen is essential for reliable in vitro and in vivo studies.
  • Standardized analytical approaches are required for comparative outcomes across different laboratories.
  • Understanding collagen features is a prerequisite for successful cell and tissue engineering applications.