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

2.5K
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...
2.5K
Structural Protein Function01:56

Structural Protein Function

27.3K
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...
27.3K
Collagens are the Major Structural Proteins of ECM01:13

Collagens are the Major Structural Proteins of ECM

4.0K
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...
4.0K

You might also read

Related Articles

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

Sort by
Same author

A cohort intervention to boost space health grant funding success for researchers from historically minoritized groups: 2022-2023.

NPJ microgravity·2026
Same author

Precision Biomaterials: Incorporating Sex, Age, and Social Descriptors in Biomaterials Research.

ACS biomaterials science & engineering·2026
Same author

Gas Chromatography-Atmospheric Pressure Chemical Ionization (GC-APCI) Expands the Analytical Window for Detection of Large PAHs (≥24 Ringed-Carbons) in Pyroplastics and Other Environmental Matrices.

ACS omega·2026
Same author

Long-Range Transport of Oil by Marine Plastic Debris: Evidence from an 8500 km Journey.

Environmental science & technology·2026
Same author

Global Voices, Shared Futures: Early-Career Scientists on the Power of Collaboration.

ACS central science·2025
Same author

Characterization of Sex-Based Differences in Integrin-Mediated Endothelial Cell Adhesion to Bioactive Hydrogels.

ACS biomaterials science & engineering·2025

Related Experiment Video

Updated: May 30, 2025

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

11.9K

Multifunctional DNA-Collagen Biomaterials: Developmental Advances and Biomedical Applications.

Nikolaos Pipis1, Bryan D James2, Josephine B Allen1,3

  • 1J. Crayton Pruitt Family Department of Biomedical Engineering, University of Florida, Gainesville, Florida 32611, United States.

ACS Biomaterials Science & Engineering
|January 27, 2025
PubMed
Summary

DNA-collagen complexes merge collagen

Keywords:
DNA aptamersDNA nanotechnologybioactive hydrogelcollagennucleic acid-collagen complexes

More Related Videos

Engineering 3D Cellularized Collagen Gels for Vascular Tissue Regeneration
09:23

Engineering 3D Cellularized Collagen Gels for Vascular Tissue Regeneration

Published on: June 16, 2015

20.8K
Production of Nanofibrillar Patterned Collagen for Tissue Engineering
07:34

Production of Nanofibrillar Patterned Collagen for Tissue Engineering

Published on: September 20, 2024

324

Related Experiment Videos

Last Updated: May 30, 2025

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

11.9K
Engineering 3D Cellularized Collagen Gels for Vascular Tissue Regeneration
09:23

Engineering 3D Cellularized Collagen Gels for Vascular Tissue Regeneration

Published on: June 16, 2015

20.8K
Production of Nanofibrillar Patterned Collagen for Tissue Engineering
07:34

Production of Nanofibrillar Patterned Collagen for Tissue Engineering

Published on: September 20, 2024

324

Area of Science:

  • Biomaterials Science
  • Regenerative Medicine
  • Molecular Biology

Background:

  • Collagen provides extracellular matrix functionality.
  • Nucleic acids offer designable bioactivity.
  • Combining them creates advanced biomaterials.

Purpose of the Study:

  • Review historical foundations and applications of DNA-collagen complexes.
  • Highlight their capabilities as platform biomaterials.
  • Discuss their potential in regenerative medicine and beyond.

Main Methods:

  • Review of existing literature on DNA-collagen complex formation and applications.
  • Analysis of structural properties across different length scales (nanoparticles, microfibers, hydrogels).
  • Examination of various nucleic acid types (siRNA, aptamers) and collagen interactions.

Main Results:

  • DNA-collagen complexes exhibit biocompatibility, bioactivity, and tunability.
  • Complex formation is controllable by component ratios and types.
  • Self-assembly of functional nucleic acids like aptamers occurs rapidly at room temperature.
  • Integration enhances biomimicry, bioactivity, and enzymatic stability.

Conclusions:

  • DNA-collagen complexes are versatile platform biomaterials.
  • They enable advances in regenerative medicine, tissue engineering, and gene delivery.
  • Their tunable nature and enhanced stability position them for broad applications including angiogenesis and wound healing.