A Novel Self-Assembled Collagenous Matrix which Serves as a Template for Oriented Growth of Hydroxyapatite Crystal

1995 ◽  
Vol 414 ◽  
Author(s):  
D. L. Christiansen ◽  
G. D. Pins ◽  
E. K. Huang ◽  
F. H. Silver
Keyword(s):  
Type I Collagen ◽  
Double Diffusion ◽  
Diffusion Chamber ◽  
Uniaxial Tensile ◽  
Type I ◽  
Oriented Growth ◽  
Selected Area Electron Diffraction ◽  
Hydroxyapatite Crystal ◽  
Self Assembled ◽  
Calcified Tissues

AbstractCollagen fibers self-assembled from solutions of molecular type I collagen were mineralized at pH 9.5, by exposure to super-saturated solutions of calcium and phosphate for a one week period in a double diffusion chamber. Uniaxial tensile mechanical properties increased with mineralization and electron microscopy of the mineral formed within the fiber was morphologically similar to the mineral phase of calcified tissues. Selected area electron diffraction confirms the presence of hydroxyapatite crystal. Further, the aligned fibrillar substructure serves as a template for the orientation of the c-axis diffraction maxima of the hydroxyapatite. These results indicate that an aligned system composed exclusively of selfassembled type I collagen fibrils serves as a scaffold for oriented growth of mineral analogous to calcification in vertebrate bone.

Development of Multilayered Chlorogenate-Peptide Based Biocomposite Scaffolds for Potential Applications in Ligament Tissue Engineering - An In Vitro Study

2017 ◽  
Vol 34 ◽  
pp. 37-56 ◽  
Author(s):  
Harrison T. Pajovich ◽  
Alexandra M. Brown ◽  
Andrew M. Smith ◽  
Sara K. Hurley ◽  
Jessica R. Dorilio ◽  
...  
Keyword(s):  
Tissue Regeneration ◽  
Type I Collagen ◽  
Phase Changes ◽  
Peptide Sequence ◽  
Proteoglycan Synthesis ◽  
Type I ◽  
Average Roughness ◽  
Potential Applications ◽  
Self Assembled

In this work, for the first time, chlorogenic acid, a natural phytochemical, was conjugated to a lactoferrin derived antimicrobial peptide sequence RRWQWRMKKLG to develop a self-assembled template. To mimic the components of extracellular matrix, we then incorporated Type I Collagen, followed by a sequence of aggrecan peptide (ATEGQVRVNSIYQDKVSL) onto the self-assembled templates for potential applications in ligament tissue regeneration. Mechanical properties and surface roughness were studied and the scaffolds displayed a Young’s Modulus of 169 MP and an average roughness of 72 nm respectively. Thermal phase changes were studied by DSC analysis. Results showed short endothermic peaks due to water loss and an exothermic peak due to crystallization of the scaffold caused by rearrangement of the components. Biodegradability studies indicated a percent weight loss of 27.5 % over a period of 37 days. Furthermore, the scaffolds were found to adhere to fibroblasts, the main cellular component of ligament tissue. The scaffolds promoted cell proliferation and displayed actin stress fibers indicative of cell motility and attachment. Collagen and proteoglycan synthesis were also promoted, demonstrating increased expression and deposition of collagen and proteoglycans. Additionally, the scaffolds exhibited antimicrobial activity against Staphylococcus epidermis bacteria, which is beneficial for minimizing biofilm formation if potentially used as implants. Thus, we have developed a novel biocomposite that may open new avenues to enhance ligament tissue regeneration.

scholarly journals Self‐Assembled Type I Collagen‐Apatite Fibers with Varying Mineralization Extent and Luminescent Terbium Promote Osteogenic Differentiation of Mesenchymal Stem Cells

2020 ◽  
pp. 2000319
Author(s):  
Ismael Romero‐Castillo ◽  
Elena López‐Ruiz ◽  
Jorge Fernando Fernández‐Sánchez ◽  
Juan Antonio Marchal ◽  
Jaime Gómez‐Morales
Keyword(s):  
Stem Cells ◽  
Mesenchymal Stem Cells ◽  
Osteogenic Differentiation ◽  
Type I Collagen ◽  
Type I ◽  
Self Assembled

Production of a Novel, Self-Assembled, Collagenous Matrix Mimicking the Hierarchical Structure of Native Aligned Connective Tissue

1995 ◽  
Vol 414 ◽  
Author(s):  
G. D. Pins ◽  
D. L. Christiansen ◽  
R. Patel ◽  
F. H. Silver
Keyword(s):  
Self Assembly ◽  
Collagen Fiber ◽  
Type I Collagen ◽  
Tensile Tests ◽  
Fiber Formation ◽  
Morphological Properties ◽  
Uniaxial Tensile ◽  
Type I ◽  
Native Collagen

AbstractThe primary goal of the biomaterials scientist and tissue engineer is to create a biocompatible implant which mimics the mechanical and morphological properties of the tissue being replaced. In vitro experimentation has documented the propensity of soluble type I collagen to self-assemble and form microscopic collagen fibrils with periodic banding analogous to native collagen fiber. Our laboratory has further investigated in vitro self-assembly by incorporating several of the “natural” processes into a multi-step fiber formation procedure which generates macroscopic collagen fiber from its molecular constituents. Results of uniaxial tensile tests and ultrastructural analyses indicate that these coextruded and stretched collagen fibers have mechanical properties and fibrillar substructure comparable to that observed in native collagen fiber.

scholarly journals Self‐Assembled Type I Collagen‐Apatite Fibers with Varying Mineralization Extent and Luminescent Terbium Promote Osteogenic Differentiation of Mesenchymal Stem Cells

2021 ◽  
Vol 21 (3) ◽  
pp. 2170006
Author(s):  
Ismael Romero‐Castillo ◽  
Elena López‐Ruiz ◽  
Jorge Fernando Fernández‐Sánchez ◽  
Juan Antonio Marchal ◽  
Jaime Gómez‐Morales
Keyword(s):  
Stem Cells ◽  
Mesenchymal Stem Cells ◽  
Osteogenic Differentiation ◽  
Type I Collagen ◽  
Type I ◽  
Self Assembled

Evaluation of biocompatibility and immunogenicity of micro/nanofiber materials based on tilapia skin collagen

2019 ◽  
Vol 33 (8) ◽  
pp. 1118-1127 ◽  
Author(s):  
Dongsheng Li ◽  
Yonglin Gao ◽  
Yunzhi Wang ◽  
Xiaoping Yang ◽  
Chuanglong He ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Helical Structure ◽  
Raw Material ◽  
Type I ◽  
Skin Collagen ◽  
Fish Collagen ◽  
Native Collagen ◽  
Mouse Immunization ◽  
Good Biocompatibility ◽  
Self Assembled

Type I collagen, used as a raw material, plays a pivotal role in the development of medical devices and tissue engineering. Due to the risk of zoonotic transmission and religious constraints for mammalian collagen, fish collagen gains increased attention and is widely seen as an alternative. In this study, two collagen micro/nanofiber materials, self-assembled collagen nanofiber and electrospun collagen nanofiber, were prepared by tilapia skin collagen and their biocompatibility and immunogenicity was thoroughly investigated. The result revealed that the state of tilapia skin collagen in self-assembled collagen nanofiber and electrospun collagen nanofiber was different. The circular dichroism spectrum indicated that collagen in self-assembled collagen nanofiber retained the triple helical structure of the native collagen, while collagen in electrospun collagen nanofiber was denatured into gelatin. Nevertheless, the evaluation according to ISO10993, including tests of cytotoxicity, hemolysis, skin sensitization, acute systemic toxicity, mouse immunization and lymphocyte proliferation, demonstrated good biocompatibility and low immunogenicity for both self-assembled and electrospun collagen nanofiber materials. Overall, the present study highlighted that type I collagen from tilapia skin would be a promising biomaterial for the development of regenerate medical products.

Biomimetic Mineralization of an Aligned, Self-Assembled Collagenous Matrix.

1991 ◽  
Vol 255 ◽  
Author(s):  
David Christiansen ◽  
Frederick H. Silver
Keyword(s):  
Mechanical Test ◽  
Double Diffusion ◽  
Diffusion Chamber ◽  
Microscopic Investigation ◽  
Collagen Fibers ◽  
Test Results ◽  
Biomimetic Mineralization ◽  
Collagenous Matrix ◽  
Self Assembled

AbstractAn in-vitro method of mineralizing an aligned, self-assembled collagenous matrix is presented. Reconstituted collagen fibers were mineralized by exposure to saturated solutions of calcium and phosphate of varying pH in a double diffusion chamber for seven days at room temperature. Microscopic investigation of the mineral precipitate within the fibers indicate the formation of hydroxyapatite crystals with features comparable to mineral observed in bone and avian tendon. Mechanical test results indicate that tensile strength and tangent modulus increase after mineralization in comparison to unmineralized control fibers. These results suggest that mineralization of collagen fiber in-vitro may parallel some of the events seen in mineralization of bone and turkey tendon. In addition, mineralized collagen fibers may be useful in the design of composites for the replacement or augmentation of hard tissue

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