Collagen Fibrils
Collagen Fibrils - Related Videos
01:11
Fibril-associated Collagen
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2023
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...
07:25
Collagen Hydrogels
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2023
Collagen is another widely used biomaterial that has found popularity in commercial applications, such as photography. Collagen has more recently been used in tissue engineering applications, by creating hydrogels that provide structure to engineered tissue. This video introduces collagen as a biomaterial, demonstrates how it is harvested from porcine skin, and shows how the material is used to create a hydrogel for tissue engineering applications. Finally, several applications of the material...
03:03
Amyloid Fibrils
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2020
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
07:54
In vitro Synthesis of Native, Fibrous Long Spacing and Segmental Long Spacing Collagen
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Cited by 16 •
2012
Simple and reproducible procedures are described for making three structurally distinct collagen assemblies from a common commercially available Type I collagen monomer. Native type, fibrous long spacing or segmental long spacing collagen can be constructed by varying the conditions to which the 300 nm long and 1.4 nm diameter monomer building block is exposed.
07:03
Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
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Cited by 18 •
2014
This procedure demonstrates in vivo near IR fluorescence imaging of collagen remodeling activities in mice as well as ex vivo staining of collagens in tissue sections using caged collagen mimetic peptides that can be photo-triggered to hybridize with denatured collagen strands.
FAQs
Fibril formation depends on collagen molecules arranging in a staggered alignment rather than simply aggregating randomly. This organization creates a structured assembly that supports the fibril’s rope-like architecture and contributes to tensile strength. In bioengineering, reproducing this arrangement is important when researchers want engineered materials to reflect the structural organization of native connective tissues.
Molecular interactions and the conditions of the surrounding matrix can influence both fibril diameter and internal organization. These variables affect how collagen molecules assemble and how the resulting fibrils develop within a material. Controlling them gives bioengineers a way to adjust the architecture of collagen-based systems rather than treating fibril structure as fixed.
Fibril architecture determines how collagen-based structures organize load-bearing elements at the nanoscale. Changes in diameter and arrangement can therefore influence the structural performance of an engineered matrix. For bioengineering, this relationship matters because tuning fibril formation can help produce scaffolds with properties better suited to replicating the organization and mechanical role of native extracellular matrix.
Adjusting fibril formation can change the matrix environment that cells encounter, including its structural organization and capacity to support cell adhesion. These changes can also influence tissue organization and degradation behavior. As a result, fibril control is not only a materials-design strategy; it is also a way to investigate how extracellular matrix architecture affects cell-matrix interactions.
Researchers use collagen fibrils both as structural models and as building blocks for biomaterials intended to replicate native extracellular matrix architecture. They can control aspects of fibril formation to tune scaffold mechanics, cell adhesion, tissue organization, and degradation. This approach connects nanoscale collagen structure with the functional requirements of engineered tissue environments.
Collagen fibril systems support the design and study of materials for regenerative medicine and engineered tissues. Their adjustable organization provides a framework for examining how scaffold structure influences mechanics, cell adhesion, tissue organization, and degradation. They are also useful for studying cell-matrix interactions, linking material architecture to biological responses in engineered environments.