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

3.6K
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...
3.6K
Type IV Collagen of Basal Lamina01:05

Type IV Collagen of Basal Lamina

3.4K
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...
3.4K
Structural Protein Function01:56

Structural Protein Function

30.5K
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...
30.5K
Glycosaminoglycans01:23

Glycosaminoglycans

7.7K
Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
7.7K
Collagens are the Major Structural Proteins of ECM01:13

Collagens are the Major Structural Proteins of ECM

6.3K
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...
6.3K

You might also read

Related Articles

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

Sort by
Same author

Ubiquitin-specific protease 11 promotes tubular cell senescence via inhibiting p53 ubiquitin degradation during renal fibrosis.

Cellular signalling·2026
Same author

Uremic toxins promote renal fatty acid synthesis and fibrosis via activating aryl hydrocarbon receptor.

Nature communications·2026
Same author

Pressure-Related Challenges and Strategic Approaches in Lithium Metal Sulfide all-Solid-State Batteries.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026
Same author

Integrated Environmental and Molecular Mechanisms of Navicula sp. Biofilm Induced Settlement and Metamorphosis in Mizuhopecten yessoensis Larvae.

Marine biotechnology (New York, N.Y.)·2026
Same author

From antibiotic impasse to cellular breakthrough: Advances in cell-based and cell-inspired strategies against bacterial infections.

Journal of controlled release : official journal of the Controlled Release Society·2026
Same author

Dual-action endoplasmic reticulum membrane-fusogenic immunogenic liposomes amplify cellular immunity in anti-tumor vaccine design.

Journal of controlled release : official journal of the Controlled Release Society·2026

Related Experiment Video

Updated: Apr 3, 2026

Generation of 3-D Collagen-based Hydrogels to Analyze Axonal Growth and Behavior During Nervous System Development
09:10

Generation of 3-D Collagen-based Hydrogels to Analyze Axonal Growth and Behavior During Nervous System Development

Published on: June 25, 2019

6.3K

Aza-Glycine Induces Collagen Hyperstability.

Yitao Zhang1, Roy M Malamakal1, David M Chenoweth1

  • 1Department of Chemistry, University of Pennsylvania , 231 South 34th Street, Philadelphia, Pennsylvania 19104-6323, United States.

Journal of the American Chemical Society
|September 15, 2015
PubMed
Summary

Synthetic chemists modified collagen by replacing glycine with aza-glycine. This substitution enhanced hydrogen bonding, creating a hyperstable triple helix, demonstrating a novel biomolecular engineering approach.

More Related Videos

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

17.9K
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

14.2K

Related Experiment Videos

Last Updated: Apr 3, 2026

Generation of 3-D Collagen-based Hydrogels to Analyze Axonal Growth and Behavior During Nervous System Development
09:10

Generation of 3-D Collagen-based Hydrogels to Analyze Axonal Growth and Behavior During Nervous System Development

Published on: June 25, 2019

6.3K
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

17.9K
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

14.2K

Area of Science:

  • Biochemistry
  • Polymer Chemistry
  • Synthetic Biology

Background:

  • Hydrogen bonding is crucial for biomolecular interactions and the stability of natural biopolymers like nucleic acids.
  • Natural biopolymers often exhibit maximized hydrogen bonding, limiting further stabilization through native modifications.
  • Glycine is the sole amino acid currently considered intolerant to substitution within the collagen structure.

Purpose of the Study:

  • To investigate the potential of synthetic modifications to enhance hydrogen bonding in biopolymers.
  • To explore the effect of substituting glycine with aza-glycine on collagen's triple-helical stability.
  • To demonstrate a method for achieving hyperstability in higher-order biopolymer systems.

Main Methods:

  • Utilized synthetic chemistry to create modified collagen peptides.
  • Introduced aza-glycine as a substitute for glycine at specific positions within the collagen sequence.
  • Analyzed the structural and stability changes in the resulting triple-helical collagen using biophysical techniques.

Main Results:

  • The substitution of glycine with aza-glycine successfully increased the number of interfacial cross-strand hydrogen bonds.
  • Modified collagen exhibited enhanced stability in its triple-helical conformation, a phenomenon termed hyperstability.
  • This modification was achieved using a minimally perturbing alternative to nature's building blocks.

Conclusions:

  • Maximizing hydrogen bonding in biopolymer systems can be effectively achieved through synthetic modifications.
  • Aza-glycine substitution represents a viable strategy for enhancing the stability of collagen and potentially other biopolymers.
  • This research opens avenues for designing novel biomaterials with improved structural integrity and function.