The properties of collagen solutions and fibres

Vasil'ev, M.P.; Vol'f, L. A.; Kotetskin, V. V.; Pukhova, Z. I.; Meos, Andres; Kutin, V. A.

doi:10.1007/bf00635776

Cited by 3 publications

(2 citation statements)

References 2 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These data suggest that there is an optimal ratio between the rate of collagen self-assembly and the shear rate. We further observed that doubling the concentration of collagen, which increases both the rate of self-assembly (29) and the viscosity of the solution (30), decreases collagen fiber alignment (fig. S7, I to L).…”

Section: Tuning Collagen Fiber Alignment and Diametermentioning

confidence: 56%

Marangoni flows drive the alignment of fibrillar cell-laden hydrogels

2020

View full text Add to dashboard Cite

When a sessile droplet containing a solute in a volatile solvent evaporates, flow in the droplet can transport and assemble solute particles into complex patterns. Transport in evaporating sessile droplets has largely been examined in solvents that undergo complete evaporation. Here, we demonstrate that flow in evaporating aqueous sessile droplets containing type I collagen—a self-assembling polymer—can be harnessed to engineer hydrated networks of aligned collagen fibers. We find that Marangoni flows direct collagen fiber assembly over millimeter-scale areas in a manner that depends on the rate of self-assembly, the relative humidity of the surrounding environment, and the geometry of the droplet. Skeletal muscle cells that are incorporated into and cultured within these evaporating droplets collectively orient and subsequently differentiate into myotubes in response to aligned networks of collagen. Our findings demonstrate a simple, tunable, and high-throughput approach to engineer aligned fibrillar hydrogels and cell-laden biomimetic materials.

show abstract

Section: Tuning Collagen Fiber Alignment and Diametermentioning

confidence: 56%

Marangoni flows drive the alignment of fibrillar cell-laden hydrogels

2020

View full text Add to dashboard Cite

show abstract

“…Vasilev et al confirmed that solutions are prone to gelation and at a temperature of 35−40 °C collagen is irreversibly destroyed as a result of the denaturation of the dissolved protein. 52 Generally, the increase of temperature induces structural transition in the collagen network which results in a shrinkage of the protein structure.…”

Section: Industrial and Engineering Chemistry Researchmentioning

confidence: 99%

Preparation and Characterization of Methyl Substituted Maleic Anhydride: Modified Collagens Destined for Medical Applications

Pamfil

Nistor

Zemljič

et al. 2014

Ind. Eng. Chem. Res.

View full text Add to dashboard Cite

Porous modified collagens with vinyl groups were synthesized by reaction with 2,3-dimethylmaleic anhydride or citraconic anhydride. The structure of modified collagen was assessed by analytical determination of the amino groups in collagen and spectroscopic methods (Fourier transform infrared (FT-IR) and proton nuclear magnetic resonance (1H NMR)). The amount of protonated amino groups and carboxylic acid moieties of the samples have been determined by potentiometric titration. The dependence of the viscosity of diluted collagen solutions on the concentration and temperature was followed to determine their denaturation transitions. The increased average molecular weight, particle size, and second virial coefficient of modified collagen solutions with respect to the unmodified one proved that modification took place. Coupled thermal analyses (TG/DTG/DTA/FT-IR/MS) also indicated the collagen modification by increased thermal stability and new volatile compounds formed during decomposition. The adhesion tests revealed their potential application in wound dressing and tissue engineering.

show abstract

Characterisation of freeze-dried type II collagen and chondroitin sulfate scaffolds

Tamaddon

Walton

Brand

et al. 2013

J Mater Sci: Mater Med

View full text Add to dashboard Cite

Collagen type-II is the dominant type of collagen in articular cartilage and chondroitin sulfate is one of the main components of cartilage extracellular matrix. Afibrillar and fibrillar type-II atelocollagen scaffolds with and without chondroitin sulfate were prepared using casting and freeze-drying methods. The scaffolds were characterised to highlight the effects of fibrillogenesis and chondroitin sulfate addition on viscosity, pore structure, porosity and mechanical properties. Microstructure analysis showed that fibrillogenesis increased the circularity of pores significantly in collagen-only scaffolds, whereas with it, no significant change was observed in chondroitin sulfate-containing scaffolds. Addition of chondroitin sulfate to afibrillar scaffolds increased the circularity of the pores and the proportion of pores between 50 and 300 μm suitable for chondrocytes growth. Fourier transform infrared spectroscopy explained the bonding between chondroitin sulfate and afibrillar collagen- confirmed with rheology results- which increased the compressive modulus 10-fold to 0.28 kPa. No bonding was observed in other scaffolds and consequently no significant changes in compressive modulus were detected.

show abstract

The properties of collagen solutions and fibres

Cited by 3 publications

References 2 publications

Marangoni flows drive the alignment of fibrillar cell-laden hydrogels

Marangoni flows drive the alignment of fibrillar cell-laden hydrogels

Preparation and Characterization of Methyl Substituted Maleic Anhydride: Modified Collagens Destined for Medical Applications

Characterisation of freeze-dried type II collagen and chondroitin sulfate scaffolds

Contact Info

Product

Resources

About