Viscoelastic Properties of Self-Assembled Type I Collagen Fibers: Molecular Basis of Elastic and Viscous Behaviors

2002 ◽  
Vol 43 (4) ◽  
pp. 569-580 ◽  
Author(s):  
Frederick H. Silver ◽  
Ali Ebrahimi ◽  
Patrick B. Snowhill
Keyword(s):  
Viscoelastic Properties ◽  
Molecular Basis ◽  
Type I Collagen ◽  
Collagen Fibers ◽  
Type I ◽  
Self Assembled

Assembly of Type I Collagen on PVA Film Induced by Glutaraldehyde Vapor

2011 ◽  
Vol 284-286 ◽  
pp. 1794-1799 ◽  
Author(s):  
Yu Lu Wang ◽  
Xue Pin Liao ◽  
Bi Shi
Keyword(s):  
Network Structure ◽  
Type I Collagen ◽  
Collagen Fibers ◽  
Type I ◽  
Collagen Concentration ◽  
Collagen Molecules ◽  
Induced Reaction ◽  
Calf Skin

Type I collagen was isolated from calf skin and its assembly on PVA film induced by glutaraldehyde vapor was investigated. It was found that the collagen molecules were firstly orientationally assembled into collagen fibers under the inducement of glutaraldehyde vapor. Then the collagen fibers could be further aggregated into novel network structure in proper conditions of the induced reaction. The morphology of the assembled collagen fibers was depended on induced time and concentration of collagen. The network arrangement could be obtained after being induced for 72h when collagen concentration was 2.5mg/ml. At higher concentration of collagen (5 mg/ml), the collagen fibers with larger dimension were obtained, but the growth of fibers was almost in one direction.

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.

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.

scholarly journals Inhibition of Collagen-Induced Platelet Aggregation by Antibodies to Distinct Types of Collagen

1977 ◽  
Author(s):  
L. Balleisen ◽  
R. Timpl ◽  
S. Gay
Keyword(s):  
Platelet Aggregation ◽  
Serum Albumin ◽  
Type I Collagen ◽  
Collagen Fibers ◽  
Type Iii Collagen ◽  
Type I ◽  
Fibrillar Collagen ◽  
Type Ii ◽  
Molecular Parameters ◽  
Inhibition Reaction

The reaction of platelets with fibrillar collagen was measured by recording aggregation according to Borns method and by retraction of Ancrod-fibrin clots. These reactions could be completely inhibited by coating the fibrils with stoichiometric amounts of purified antibodies to type I, II or III collagens. The inhibition was specific, i. e. antibodies to type I collagen prevented aggregation by type I collagen but not by type II or III collagen. Comparable amounts ofantibodies to fibrinogen or to serum albumin had no effect on the reaction. The data indicate that platelet aggregation by type I or II collagen fibrils is not due to contamination with type III collagen. The inhibition reaction may be useful for further studies on molecular parameters of the interaction between platelets and collagen fibers.

Hydrogen peroxide-induced degradation of type I collagen fibers of tilapia skin

2014 ◽  
Vol 2 (1-2) ◽  
pp. 41-48 ◽  
Author(s):  
Xiaoling Liu ◽  
Yuanxin Jiang ◽  
Hong He ◽  
Wei Ping
Keyword(s):  
Hydrogen Peroxide ◽  
Type I Collagen ◽  
Collagen Fibers ◽  
Type I

scholarly journals Incorporation of Superparamagnetic Iron Oxide Nanoparticles into Collagen Formulation for 3D Electrospun Scaffolds

Nanomaterials ◽  
2022 ◽  
Vol 12 (2) ◽  
pp. 181
Author(s):  
Manuel Estévez ◽  
Giorgia Montalbano ◽  
Alvaro Gallo-Cordova ◽  
Jesús G. Ovejero ◽  
Isabel Izquierdo-Barba ◽  
...  
Keyword(s):  
Iron Oxide ◽  
Iron Oxide Nanoparticles ◽  
Type I Collagen ◽  
Superparamagnetic Iron Oxide ◽  
Collagen Fibers ◽  
Superparamagnetic Iron Oxide Nanoparticles ◽  
Biological Assessment ◽  
Oxide Nanoparticles ◽  
Type I ◽  
Electrospun Scaffolds

Nowadays, there is an ever-increasing interest in the development of systems able to guide and influence cell activities for bone regeneration. In this context, we have explored for the first time the combination of type-I collagen and superparamagnetic iron oxide nanoparticles (SPIONs) to design magnetic and biocompatible electrospun scaffolds. For this purpose, SPIONs with a size of 12 nm were obtained by thermal decomposition and transferred to an aqueous medium via ligand exchange with dimercaptosuccinic acid (DMSA). The SPIONs were subsequently incorporated into type-I collagen solutions to prove the processability of the resulting hybrid formulation by means of electrospinning. The optimized method led to the fabrication of nanostructured scaffolds composed of randomly oriented collagen fibers ranging between 100 and 200 nm, where SPIONs resulted distributed and embedded into the collagen fibers. The SPIONs-containing electrospun structures proved to preserve the magnetic properties of the nanoparticles alone, making these matrices excellent candidates to explore the magnetic stimuli for biomedical applications. Furthermore, the biological assessment of these collagen scaffolds confirmed high viability, adhesion, and proliferation of both pre-osteoblastic MC3T3-E1 cells and human bone marrow-derived mesenchymal stem cells (hBM-MSCs).

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