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Related Concept Videos

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...
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
The Structure of Intermediate Filaments01:19

The Structure of Intermediate Filaments

The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm).  These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
Intermediate filaments...
Formation of Intermediate Filaments00:57

Formation of Intermediate Filaments

Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been reported.
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...
Fiber Reinforced Concrete01:22

Fiber Reinforced Concrete

Fiber-reinforced concrete significantly enhances the structural and nonstructural properties of traditional concrete by incorporating fibers like steel, glass, and polymers. These fibers, varying from natural ones such as sisal and cellulose to manufactured ones like polypropylene and Kevlar, are mixed into hydraulic cement with aggregates. Steel fibers, often preferred for their robustness, contribute to improved ductility, toughness, and post-cracking performance. The concrete is classified...

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Encapsulation of Cardiomyocytes in a Fibrin Hydrogel for Cardiac Tissue Engineering
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Technological advances in fibrin for tissue engineering.

Raúl Sanz-Horta1, Ana Matesanz2,3, Alberto Gallardo1

  • 1Department of Applied Macromolecular Chemistry, Institute of Polymer Science and Technology, Spanish National Research Council (ICTP-CSIC), Madrid, Spain.

Journal of Tissue Engineering
|August 17, 2023
PubMed
Summary
This summary is machine-generated.

Fibrin hydrogels show promise in tissue engineering but require improvements in stability and mechanical strength. This review explores modifications like composite scaffolds and interpenetrated polymer networks to enhance fibrin-based biomaterials.

Keywords:
Fibrin hydrogels in tissue engineeringPEGylated fibrin hydrogelsfibrin-polymer composite scaffoldsnatural polymer-fibrin hydrogelsparticles encapsulated in fibrin hydrogels

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Area of Science:

  • Biomaterials Science
  • Polymer Chemistry
  • Tissue Engineering

Background:

  • Fibrin is a versatile natural polymer utilized in biomedical applications, including hemostatic agents, drug/cell delivery, and tissue engineering scaffolds.
  • Current limitations of fibrin hydrogels include rapid degradation, shrinkage, poor mechanical properties, and batch variability, hindering broader clinical adoption.
  • Modifying fibrin's structure and composition is crucial for enhancing its performance in bioengineering.

Purpose of the Study:

  • To critically review recent advancements in modifying fibrin hydrogels for improved performance.
  • To focus on composite fibrin scaffolds, chemically modified hydrogels, and interpenetrated polymer networks (IPNs) for tissue engineering applications.

Main Methods:

  • Review of literature on fibrin hydrogel modifications.
  • Analysis of composite fibrin scaffolds incorporating other natural or synthetic materials.
  • Examination of chemically modified fibrin hydrogels.
  • Investigation of interpenetrated polymer networks (IPNs) combining fibrin with other polymers.

Main Results:

  • Composite fibrin scaffolds demonstrate enhanced mechanical properties and controlled degradation rates.
  • Chemical modifications can improve fibrin's stability and cell compatibility.
  • IPN hydrogels offer tunable properties by integrating fibrin with synthetic or natural polymers, leading to improved structural integrity.
  • These modifications collectively address the limitations of native fibrin for tissue engineering.

Conclusions:

  • Advanced fibrin-based biomaterials, including composites, chemically modified hydrogels, and IPNs, show significant potential for tissue engineering.
  • Strategic modifications are key to overcoming the inherent limitations of fibrin, paving the way for more reliable and effective biomedical applications.
  • Further research into these enhanced fibrin materials will accelerate their translation into clinical practice.