The formation of fibrils from collagen solutions 1. The effect of experimental conditions: kinetic and electron-microscope studies

Wood, G. C.; Keech, M. K.

doi:10.1042/bj0750588

Cited by 420 publications

(279 citation statements)

References 28 publications

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“…Considering that the conclusions of these authors were consistent with the results concerning the kinetics of gelation of samples prepared at pH 7, it was chosen not to report them here in detail. In general, turbidity assays have already been used to assess collagen self-assembly in vitro [23,24,30,31] This work studied collagen gels prepared at a higher concentration (2.8 mg/mL) and a higher pH (10) than those discussed by the previously cited authors, and the results concerning the effects of temperature and ionic strength are consistent with both these works. In the case of the effect of pH, the results presented here agree with the conclusions from Wood et al [23].…”

Section: Turbidity Measurementssupporting

confidence: 80%

“…In general, turbidity assays have already been used to assess collagen self-assembly in vitro [23,24,30,31] This work studied collagen gels prepared at a higher concentration (2.8 mg/mL) and a higher pH (10) than those discussed by the previously cited authors, and the results concerning the effects of temperature and ionic strength are consistent with both these works. In the case of the effect of pH, the results presented here agree with the conclusions from Wood et al [23]. All the factors had a statistically significant effect on gelation, in terms of kinetics or final absorbance (p < 0.05).…”

Section: Turbidity Measurementssupporting

confidence: 80%

“…Results from the turbidity measurements as a function of pH (7,10), ionic strength (c1, c2, c3, c4, c5, c6, c7) and temperature (T1 = 4 °C, T1* = 4 °C and 21 °C after 38 days, T2 = 21 °C, T3 = 37 °C): Final absorbance for all the types of gels and t 1/2 for gels prepared at pH 10. The kinetics of gels prepared at pH 7 as a function of collagen concentration, temperature and ionic strength has already been widely discussed by several authors [23,24,30,31]. Considering that the conclusions of these authors were consistent with the results concerning the kinetics of gelation of samples prepared at pH 7, it was chosen not to report them here in detail.…”

Section: Turbidity Measurementssupporting

confidence: 66%

“…Ionization and electrostatic interactions between amino acid residues are regulated by factors such as pH and ionic strength. The formation of net charges between collagen molecules of neighboring fibrils may determine electrostatic attractions that can stabilize the matrix as well as affect the size of the fibrils and consequently the structure of the matrix [20][21][22][23]. Moreover, temperature affects the hydrophobic interactions and therefore the kinetics of collagen fibrillogenesis as well as pH and ionic strength [20,23,24].…”

Section: Introductionmentioning

confidence: 99%

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Tailoring Mechanical Properties of Collagen-Based Scaffolds for Vascular Tissue Engineering: The Effects of pH, Temperature and Ionic Strength on Gelation

2010

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Collagen gels have been widely studied for applications in tissue engineering because of their biological implications. Considering their use as scaffolds for vascular tissue engineering, the main limitation has always been related to their low mechanical properties. During the process of in vitro self-assembly, which leads to collagen gelation, the size of the fibrils, their chemical interactions, as well as the resulting microstructure are regulated by three main experimental conditions: pH, ionic strength and temperature. In this work, these three parameters were modulated in order to increase the mechanical properties of collagen gels. The effects on the gelation process were assessed by turbidimetric and scanning electron microscopy analyses. Turbidity measurements showed that gelation was affected by all three factors and scanning electron images confirmed that major changes occurred at the microstructural level. Mechanical tests showed that the compressive and tensile moduli increased by four-and three-fold, respectively, compared to the control. Finally, viability tests confirmed that these gels are suitable as scaffolds for cellular adhesion and proliferation.

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Section: Turbidity Measurementssupporting

confidence: 80%

Section: Turbidity Measurementssupporting

confidence: 80%

Section: Turbidity Measurementssupporting

confidence: 66%

Section: Introductionmentioning

confidence: 99%

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Tailoring Mechanical Properties of Collagen-Based Scaffolds for Vascular Tissue Engineering: The Effects of pH, Temperature and Ionic Strength on Gelation

2010

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“…Collagen self-polymerizes in a two-phase process (nucleation/growth [20,22] ) which is determined by pH, temperature, and polymerization rate [23][24][25][26] . The highlytunable mechanical properties [27,28] and swelling of fibers [28] allow collagen to form a hydrogel.…”

Section: Polymersmentioning

confidence: 99%

Biomaterials for spinal cord repair

Haggerty

Oudega

2013

Neurosci. Bull.

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Spinal cord injury (SCi) results in permanent loss of function leading to often devastating personal, economic and social problems. A contributing factor to the permanence of SCi is that damaged axons do not regenerate, which prevents the re-establishment of axonal circuits involved in function. Many groups are working to develop treatments that address the lack of axon regeneration after SCi. The emergence of biomaterials for regeneration and increased collaboration between engineers, basic and translational scientists, and clinicians hold promise for the development of effective therapies for SCi. A plethora of biomaterials is available and has been tested in various models of SCi. Considering the clinical relevance of contusion injuries, we primarily focus on polymers that meet the specific criteria for addressing this type of injury. Biomaterials may provide structural support and/or serve as a delivery vehicle for factors to arrest growth inhibition and promote axonal growth. Designing materials to address the specific needs of the damaged central nervous system is crucial and possible with current technology. Here, we review the most prominent materials, their optimal characteristics, and their potential roles in repairing and regenerating damaged axons following SCi.Keywords: spinal cord injury; axon regeneration; biodegradable materials; extracellular matrix proteins; functional recovery; growth factor; guidance; injury and repair; spinal motor neuron IntroductionSpinal cord injury (SCi) causes loss of neurons and axons resulting in motor and sensory function impairments. There are thousands of new cases of SCi in the world annually [1,2] occurring often in young adults. The lack of endogenous repair and the significant costs to the individual, family and society [1] are important motivations behind the continuing efforts to develop effective therapies. Promoting axonal regeneration is considered a potential repair strategy because it could lead to recovery of axonal circuits involved in motor and/or sensory function [3] .The central nervous system (CNS) neurons are intrinsically capable of some regeneration of damaged axons [4] but their attempts after SCi are frustrated by structural and chemical obstructions in the damaged nervous tissue [5] . Spinal cord repair approaches typically lead to small functional gains. one feature that most of these approaches have in common is a poor axonal regeneration response, suggesting that promoting axonal regeneration, including synapse formation, is essential to achieve substantial functional repair after SCi. if so, it is rational to anticipate that effective spinal cord therapies will need to include interventions addressing the axon growth-inhibition that leads to the poor axonal growth responses. As introduced above, axonal regeneration is considered an important repair mechanism for the injured spinal cord. Therefore, this review focuses on materials that have shown most promise to elicit an axonal regeneration response to foster functional restoration after ...

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Viscosity and elasticity during collagen assembly in vitro: Relevance to matrix-driven translocation

et al. 1997

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The formation of fibrils from collagen solutions 1. The effect of experimental conditions: kinetic and electron-microscope studies

Cited by 420 publications

References 28 publications

Tailoring Mechanical Properties of Collagen-Based Scaffolds for Vascular Tissue Engineering: The Effects of pH, Temperature and Ionic Strength on Gelation

Tailoring Mechanical Properties of Collagen-Based Scaffolds for Vascular Tissue Engineering: The Effects of pH, Temperature and Ionic Strength on Gelation

Biomaterials for spinal cord repair

Viscosity and elasticity during collagen assembly in vitro: Relevance to matrix-driven translocation

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