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Related Concept Videos

Fibrous Proteins00:55

Fibrous Proteins

Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
Extracellular Matrix01:26

Extracellular Matrix

Unlike epithelial tissue, which is composed of cells closely packed with little or no extracellular space in between, connective tissue cells are dispersed in a matrix. This extracellular matrix (ECM) is composed of fibrous proteins like collagen, elastin, and fibronectin in a ground substance consisting of interstitial fluid, cell adhesion proteins, and proteoglycans. The proteoglycans form a gel-like material in the spaces between cells and provide hydration, buffering, binding, and force...
Fibronectins Connect Cells with ECM01:25

Fibronectins Connect Cells with ECM

Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Tissue Renewal without Stem Cells01:23

Tissue Renewal without Stem Cells

After cellular or tissue damage, the resident stem cells present in the human body can locally repair and regenerate the damaged tissue or organ. However, even though some tissues do not have stem cells, they can repair and regenerate with the help of pre-existing cells. For example, beta cells of the pancreas and hepatocytes of the liver can divide to renew and regenerate the tissue. Here, both cell division and cell death are well regulated by homeostasis.
However, failure of such a system...

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Core/shell Printing Scaffolds For Tissue Engineering Of Tubular Structures
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Aligned core-shell nanofibers delivering bioactive proteins.

I C Liao1, S Y Chew, K W Leong

  • 1Department of Biomedical Engineering, Duke University, Durham, NC 27708, USA.

Nanomedicine (London, England)
|August 25, 2007
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Summary

This study demonstrates co-axial electrospinning for creating protein-releasing nanofibers for tissue engineering. Poly(ethylene glycol) controls release, enabling sustained delivery of growth factors for regenerative medicine.

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Area of Science:

  • Biomaterials Science
  • Tissue Engineering
  • Regenerative Medicine

Background:

  • Continuous nanostructures can deliver topographical and biochemical cues for tissue regeneration.
  • Co-axial electrospinning offers a method to embed proteins within nanofibers.

Purpose of the Study:

  • To develop aligned nanofibers using co-axial electrospinning encapsulating bovine serum albumin (BSA) and platelet-derived growth factor-bb (PDGF-bb).
  • To demonstrate controlled release of BSA and bioactivity retention of PDGF-bb.
  • To explore applications in regenerative medicine.

Main Methods:

  • Co-axial electrospinning of poly(epsilon-caprolactone) (PCL) nanofibers.
  • Incorporation of poly(ethylene glycol) (PEG) as a porogen in the PCL shell for controlled release.
  • Encapsulation of BSA and PDGF-bb within the nanofibers.

Main Results:

  • BSA release half-lives ranged from 1 to 20 days, dependent on PEG concentration and molecular weight.
  • Optimized PDGF-bb-loaded nanofibers achieved complete release with near zero-order kinetics.
  • Preserved bioactivity of PDGF-bb was confirmed.

Conclusions:

  • Co-axial electrospinning is a versatile technique for controlled delivery of biochemical signals.
  • This approach holds promise for tissue engineering and regenerative medicine applications.