Injectable collagen as a pH-sensitive hydrogel

Rosenblatt, Joel; Devereux, Brian M.; Wallace, Donald G.

doi:10.1016/0142-9612(94)90079-5

Cited by 104 publications

(74 citation statements)

References 24 publications

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“…Some of them already pointed out that, regarding the process of self-assembly, the modulation of these parameters can determine modifications at the micro-structural level in terms of the fibril size and the electrostatic interactions between neighboring fibrils [20,21,23,[33][34][35]38]. Roeder et al showed, in agreement with the conclusions from Wood et al, that the fibril diameter decreases and the fibril length increases by increasing the pH, conjecturing that this change could explain the improvement in the mechanical properties [21,23].…”

Section: (Kpa)supporting

confidence: 76%

“…The matrices appear tighter at higher pH for all the considered levels of ionic strength. The same observation can be found in the work of Rosenblatt et al [20]. This effect is probably due to the formation of net electrostatic interactions between charged residues, resulting in tighter packing of the fibrils.…”

Section: Semsupporting

confidence: 75%

“…This effect can be considered in terms of an increase of hydrophobic interactions due to an increase of temperature. As well, a decrease of ionic strength can prevent the phenomenon of salting in and enhance bonding between electrostatically charged amino acid side chains [20]. The difference in the gelation rate in some cases could be observed macroscopically by the presence of bubbles that generally remained trapped in the gel when gelation was completed in less than one hour.…”

Section: Turbidity Measurementsmentioning

confidence: 99%

“…Collagen fibrillogenesis depends on electrostatic and hydrophobic interactions [11,[17][18][19][20]. Ionization and electrostatic interactions between amino acid residues are regulated by factors such as pH and ionic strength.…”

Section: Introductionmentioning

confidence: 99%

“…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: (Kpa)supporting

confidence: 76%

Section: Semsupporting

confidence: 75%

Section: Turbidity Measurementsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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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pH and Thrombin Concentration Are Decisive in Synthesizing Stiff, Stable, and Open‐Porous Fibrin‐Collagen Hydrogel Blends without Chemical Cross‐Linker

Wachendörfer

Buhl

Messaoud

et al. 2023

Adv Healthcare Materials

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Fibrin‐collagen hydrogel blends exhibit high potential for tissue engineering applications. However, it is still unclear whether the underlying cross‐linking mechanisms are of chemical or physical nature. It is here hypothesized that chemical cross‐linkers play a negligible role and that instead pH and thrombin concentration are decisive for synthetizing blends with high stiffness and hydrolytic stability. Different fibrin‐collagen formulations (pure and with additional transglutaminase) are used and the blends’ compaction rate, hydrolytic stability, compressive strength, and hydrogel microstructure are investigated. The effect of thrombin concentration on gel compaction is examined and the importance of pH control during synthesis observed. It is revealed that transglutaminase impairs gel stability and it is deduced that fibrin‐collagen blends mainly cross‐link by mechanical interactions due to physical fibril entanglement as opposed to covalent bonds from chemical cross‐linking. High thrombin concentrations and basic pH during synthesis reduce gel compaction and enhance stiffness and long‐term stability. Scanning electron microscopy reveals a highly interpenetrating fibrous network with unique, interconnected open‐porous microstructures. Endothelial cells proliferate on the blends and form a confluent monolayer. This study reveals the underlying cross‐linking mechanisms and presents enhanced fibrin‐collagen blends with high stiffness, hydrolytic stability, and large, interconnected pores; findings that offer high potential for advanced tissue engineering applications.

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Injectable Superparamagnetic Ferrogels for Controlled Release of Hydrophobic Drugs

et al. 2009

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A ferrogel for magnetically controlled release of drugs is prepared by integration of superparamagnetic iron oxide nanoparticles and Pluronic F127 gels. The hydrophobic drug indomethacin is loaded in the ferrogel owing to the oil‐in‐water micellar structure. The characteristic sol–gel transition property renders the ferrogel an injectable drug carrier that will be, in principle, free from surgical implant procedure.

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Injectable collagen as a pH-sensitive hydrogel

Cited by 104 publications

References 24 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

pH and Thrombin Concentration Are Decisive in Synthesizing Stiff, Stable, and Open‐Porous Fibrin‐Collagen Hydrogel Blends without Chemical Cross‐Linker

Injectable Superparamagnetic Ferrogels for Controlled Release of Hydrophobic Drugs

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