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Related Concept Videos

Collagens are the Major Structural Proteins of ECM01:13

Collagens are the Major Structural Proteins of ECM

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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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The Nucleosome Core Particle02:10

The Nucleosome Core Particle

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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
The paradox
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The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
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Fibril-associated Collagen01:11

Fibril-associated Collagen

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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...
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Viral Structure00:56

Viral Structure

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Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.
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Protein and Protein Structure02:15

Protein and Protein Structure

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
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Related Experiment Video

Updated: Feb 11, 2026

Tri-layered Electrospinning to Mimic Native Arterial Architecture using Polycaprolactone, Elastin, and Collagen: A Preliminary Study
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Tri-layered Electrospinning to Mimic Native Arterial Architecture using Polycaprolactone, Elastin, and Collagen: A Preliminary Study

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Native collagen hydrogel nanofibres with anisotropic structure using core-shell electrospinning.

Yuka Wakuda1, Shohei Nishimoto1, Shin-Ichiro Suye1,2

  • 1Department of Frontier Fibre Technology and Science, Graduate School of Engineering, University of Fukui, Fukui, 910-8507, Japan.

Scientific Reports
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PubMed
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Researchers developed a novel method to create anisotropic collagen hydrogel nanofibers without cross-linking. This technique mimics native extracellular matrix (ECM) structure, advancing regenerative medicine materials.

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Fabricating Degradable Thermoresponsive Hydrogels on Multiple Length Scales via Reactive Extrusion, Microfluidics, Self-assembly, and Electrospinning
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In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
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Tri-layered Electrospinning to Mimic Native Arterial Architecture using Polycaprolactone, Elastin, and Collagen: A Preliminary Study
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In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
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In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen

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Area of Science:

  • Biomaterials Science
  • Regenerative Medicine
  • Tissue Engineering

Background:

  • Collagen hydrogels are widely used in regenerative medicine but typically exhibit isotropic structures, unlike anisotropic native extracellular matrix (ECM).
  • Current methods for fabricating anisotropic collagen nanofibers, such as electrospinning from organic solvents, yield water-soluble fibers requiring cross-linking for scaffold applications.

Purpose of the Study:

  • To develop a method for fabricating anisotropic collagen hydrogel nanofibers from an aqueous solution without chemical or thermal cross-linking.
  • To create biomaterials that mimic the anisotropic structure of native ECM for improved cell culture and tissue regeneration.

Main Methods:

  • Utilized a core-shell electrospinning technique with an aqueous acidic collagen solution as the core and polyvinylpyrrolidone (PVP) as the shell.
  • Gelled the core collagen and subsequently removed the PVP shell using a basic ethanol solution to yield anisotropic collagen hydrogel nanofibers.
  • Characterized the resulting fibers using immunostaining, Fourier transform infrared spectroscopy, and circular dichroism to confirm collagen composition and structure.

Main Results:

  • Successfully fabricated anisotropic collagen hydrogel nanofibers from an aqueous solution.
  • Confirmed the fibers were composed of collagen with intact triple helical structures and complete removal of the PVP shell.
  • Demonstrated that human umbilical vein endothelial cells cultured on the fibers aligned with the fiber direction, indicating anisotropic guidance.

Conclusions:

  • The core-shell electrospinning method provides a viable route to produce anisotropic collagen hydrogel nanofibers without cross-linking.
  • This technique offers a safer alternative for developing biomaterials with native-like ECM anisotropy, suitable for regenerative medicine applications.
  • The developed method facilitates the creation of advanced scaffolds that can guide cell behavior and promote tissue regeneration.