Collagen Monomer
Collagen Monomer - Related Videos
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...
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.
09:47
Isolation and Compositional Analysis of Plant Cuticle Lipid Polyester Monomers
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Cited by 32 •
2015
Lipid polyesters constitute the structural components of two cell wall modifications, the plant cuticle and suberin-containing diffusion barriers. In this video, we describe a method to depolymerize cutin from whole delipidated leaves. The method can be applied to investigating mutants compromised in either cutin or suberin biosynthesis.
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.
09:02
Using Polystyrene-block-poly(acrylic acid)-coated Metal Nanoparticles as Monomers for Their Homo- and Co-polymerization
0 Views •
Cited by 1 •
2015
We report protocols for “polymerizing” various types of polymer-encapsulated metal nanoparticles into long chains of “homo-“ and “co-polymers”.
FAQs
After triple-helix units are available, they can align and self-assemble into larger fibrils. Intermolecular crosslinking then connects neighboring collagen molecules, helping stabilize the assembled structure and increase tissue strength. In bioengineering, this sequence matters because researchers can treat fibril formation and crosslinking as separate design stages when constructing collagen-based materials with targeted structural and mechanical behavior.
Monomer concentration and assembly conditions determine how readily the molecules organize into fibrils and what resulting material characteristics emerge. Adjusting these variables gives researchers a way to control the structure formed before additional crosslinking. This control is important when the same collagen building block must be adapted to different biomaterial formats, including hydrogels and porous scaffolds.
Crosslinking connects collagen molecules within the assembled structure, providing greater strength and stability than alignment and fibril formation alone. In engineered systems, the extent of crosslinking is therefore a key control point rather than a minor finishing step. It can be adjusted alongside assembly conditions to help tune mechanical properties, degradation behavior, and cellular interactions.
The organization of three alpha chains into a triple helix provides a defined molecular unit that can participate in higher-order assembly. That hierarchy links molecular design to fibril structure and, ultimately, to the performance of a collagen material. Bioengineers can therefore evaluate both monomer-level organization and subsequent assembly when designing extracellular-matrix-inspired systems.
Researchers begin with purified or recombinant collagen monomers, select a target format such as a hydrogel or porous scaffold, and control monomer concentration and assembly conditions. After fibril formation, they can introduce or regulate intermolecular crosslinking. The resulting material is then considered in terms of mechanical properties, degradation, and cellular interactions relevant to its intended use.
Purified and recombinant forms provide collagen building blocks that can be incorporated into engineered environments. Their use supports construction of hydrogels, porous scaffolds, and other biomaterials. This flexibility allows collagen-based systems to be selected for tissue engineering, wound repair, or cell culture applications, where researchers can adjust assembly and crosslinking to influence material behavior.