Type I Collagen Self-Assembly: The Roles of Substrate and Concentration

Langmuir ◽  
2013 ◽  
Vol 29 (7) ◽  
pp. 2330-2338 ◽  
Author(s):  
Ming Fang ◽  
Elizabeth L. Goldstein ◽  
Eryn K. Matich ◽  
Bradford G. Orr ◽  
Mark M. Banaszak Holl
Keyword(s):  
Self Assembly ◽  
Type I Collagen ◽  
Type I

scholarly journals Increased Fibroblast Metabolic Activity of Collagen Scaffolds via the Addition of Propolis Nanoparticles

Materials ◽  
2020 ◽  
Vol 13 (14) ◽  
pp. 3118
Author(s):  
Jeimmy González-Masís ◽  
Jorge M. Cubero-Sesin ◽  
Yendry R. Corrales-Ureña ◽  
Sara González-Camacho ◽  
Nohelia Mora-Ugalde ◽  
...  
Keyword(s):  
Metabolic Activity ◽  
Self Assembly ◽  
Type I Collagen ◽  
Fibroblast Cell ◽  
Antimicrobial Activities ◽  
Hydrodynamic Diameter ◽  
Type I ◽  
Collagen Scaffolds ◽  
Simple Method ◽  
Socially Relevant

Propolis natural extracts have been used since ancient times due to their antioxidant, anti-inflammatory, antiviral, and antimicrobial activities. In this study, we produced scaffolds of type I collagen, extracted from Wistar Hanover rat tail tendons, and impregnated them with propolis nanoparticles (NPs) for applications in regenerative medicine. Our results show that the impregnation of propolis NPs to collagen scaffolds affected the collagen denaturation temperature and tensile strength. The changes in structural collagen self-assembly due to contact with organic nanoparticles were shown for the first time. The fibril collagen secondary structure was preserved, and the D-pattern gap increased to 135 ± 28 nm, without losing the microfiber structure. We also show that the properties of the collagen scaffolds depended on the concentration of propolis NPs. A concentration of 100 μg/mL of propolis NPs with 1 mg of collagen, with a hydrodynamic diameter of 173 nm, was found to be an optimal concentration to enhance 3T3 fibroblast cell metabolic activity and cell proliferation. The expected outcome from this research is both scientifically and socially relevant since the home scaffold using natural nanoparticles can be produced using a simple method and could be widely used for local medical care in developing communities.

scholarly journals Self-assembly study of type I collagen extracted from male Wistar Hannover rat tail tendons

2020 ◽  
Vol 24 (1) ◽  
Author(s):  
Jeimmy González-Masís ◽  
Jorge M. Cubero-Sesin ◽  
Simón Guerrero ◽  
Sara González-Camacho ◽  
Yendry Regina Corrales-Ureña ◽  
...  
Keyword(s):  
Regenerative Medicine ◽  
Self Assembly ◽  
Type I Collagen ◽  
Ph Effect ◽  
The Self ◽  
Titration Calorimetry ◽  
Type I ◽  
Self Assembling ◽  
Functional Features ◽  
Rat Tail

Abstract Background Collagen, the most abundant protein in the animal kingdom, represents a promising biomaterial for regenerative medicine applications due to its structural diversity and self-assembling complexity. Despite collagen’s widely known structural and functional features, the thermodynamics behind its fibrillogenic self-assembling process is still to be fully understood. In this work we report on a series of spectroscopic, mechanical, morphological and thermodynamic characterizations of high purity type I collagen (with a D-pattern of 65 nm) extracted from Wistar Hannover rat tail. Our herein reported results can be of help to elucidate differences in self-assembly states of proteins using ITC to improve the design of energy responsive and dynamic materials for applications in tissue engineering and regenerative medicine. Methods Herein we report the systematic study on the self-assembling fibrillogenesis mechanism of type I collagen, we provide morphological and thermodynamic evidence associated to different self-assembly events using ITC titrations. We provide thorough characterization of the effect of pH, effect of salts and protein conformation on self-assembled collagen samples via several complementary biophysical techniques, including circular dichroism (CD), Fourier Transform infrared spectroscopy (FTIR), differential scanning calorimetry (DSC), atomic force microscopy (AFM), scanning electron microscopy (SEM), dynamic mechanical thermal analysis (DMTA) and thermogravimetric analysis (TGA). Results Emphasis was made on the use of isothermal titration calorimetry (ITC) for the thermodynamic monitoring of fibrillogenesis stages of the protein. An overall self-assembly enthalpy value of 3.27 ± 0.85 J/mol was found. Different stages of the self-assembly mechanism were identified, initial stages take place at pH values lower than the protein isoelectric point (pI), however, higher energy release events were recorded at collagen’s pI. Denatured collagen employed as a control exhibited higher energy absorption at its pI, suggesting different energy exchange mechanisms as a consequence of different aggregation routes. Graphical abstract

Surface Modification of Polydimethylsiloxane Using Low Pressure Chemical Vapour Deposition of Poly-Chloro-p-Xylene

2012 ◽  
Vol 20 ◽  
pp. 129-142 ◽  
Author(s):  
Paul Emile Poleni ◽  
Nazare Pereira-Rodrigues ◽  
Denis Guimard ◽  
Yasuhiko Arakawa ◽  
Yasuyuki Sakai ◽  
...  
Keyword(s):  
Tissue Engineering ◽  
Self Assembly ◽  
Vapour Deposition ◽  
Type I Collagen ◽  
Chemical Vapour ◽  
The Self ◽  
Type I ◽  
Liver Tissue Engineering ◽  
Pressure Chemical ◽  
Huvec Cells

The capability to understand and modulate accurately the self-assembly of the extracellular matrix (ECM) components still one of the major fundamental objectives in the field of liver tissue engineering. In the present study, we put in evidence the suitability of poly-chloro-p-xylene (Parylene-C, ParC) for modulating the self-assembly of ECM (type-I collagen) microenvironment and cellular topography of human hepatocarcinoma (HepG2) and Human umbilical vascular endothelial (HUVEC) cells while coated on a polydimethylsiloxane (PDMS) substratum. Our findings demonstrated that the wettability of PDMS and ParC/PDMS were identical, while ParC/PDMS was significantly rougher than PDMS before and after collagen coating. However, the roughness and the wettability of ParC/PDMS were comparable to those of polystyrene (PS), a substratum commonly used for in vitro biological-related investigations. Type-I collagen adsorbed on ParC/PDMS and PS exhibited a dense network of microstructures around ~1 nm high and ~30-50 nm wide, whereas collagen adsorbed on PDMS had a low surface density of elongated fibrils that were ~2 nm thick and ~200 nm wide. This disparity in ECM microarchitecture leaded to distinct culture topographies of HepG2 cells (3D and 2D for PDMS and ParC/PDMS, respectively) and viability of HUVEC (2D viable HUVEC cells and non attached dead cells on ParC/PDMS and PDMS, respectively). To conclude, the observed changes in cell morphology and viability between ParC/PDMS and PDMS alone were directly related to the nature of the material which may impact the supramolecular organization of adsorbed ECM. We strongly believe that Low Pressure Chemical Vapour deposition (LPCVD) of ParC will offer promising insights into how microscale ECM modifications directly impact cell morphology and activity, leading to the development of advanced micro/nanosized tissue-engineered ParC/PDMS patterns with applications for liver tissue engineering.

Influence of Mechanical Load on the Degradation of Corneal Collagen

2008 ◽  
Author(s):  
Ramin Zareian ◽  
Kelli P. Church ◽  
Jeffrey W. Ruberti
Keyword(s):  
Self Assembly ◽  
Type I Collagen ◽  
Mechanical Load ◽  
Structural Performance ◽  
Type I ◽  
Connective Tissues ◽  
Bacterial Collagenase ◽  
Collagen Triple Helix ◽  
Different Types ◽  
Corneal Collagen

Collagen is one of the most important structural proteins in vertebrate animals. Over 25 different types of collagen have been identified, but type I collagen is the most abundant fibril forming collagen and contributes to the structural performance numerous connective tissues including ligaments, tendons and cornea [1]. In addition to collagen self-assembly, collagen degradation is an important step in the development, remodeling, homeostasis and pathology of load-bearing ECM. Matrix Metalloproteinase (MMP) types I and VIII, bacterial collagenase and cathepsin are the best known enzymes capable of directly degrading the collagen triple helix [2, 3]. Several researchers have hypothesized that straining collagen fibrils makes them less susceptible to enzymatic degradation [4, 5]. This concept, which we refer to as “strain-stabilization” has important implications for our understanding of collagen as an engineering material.

scholarly journals The Characteristics of Intrinsic Fluorescence of Type I Collagen Influenced by Collagenase I

2018 ◽  
Vol 8 (10) ◽  
pp. 1947 ◽  
Author(s):  
Yiming Shen ◽  
Deyi Zhu ◽  
Wenhui Lu ◽  
Bing Liu ◽  
Yanchun Li ◽  
...  
Keyword(s):  
Fluorescence Intensity ◽  
Self Assembly ◽  
Triple Helix ◽  
Type I Collagen ◽  
Intrinsic Fluorescence ◽  
Type I ◽  
Food And Agriculture ◽  
Mechanism Research ◽  
Helix Structure ◽  
Assembly Behavior

The triple helix structure of collagen can be degraded by collagenase. In this study, we explored how the intrinsic fluorescence of type I collagen was influenced by collagenase I. We found that tyrosine was the main factor that could successfully excite the collagen fluorescence. Initially, self-assembly behavior of collagen resulted in a large amount of tyrosine wrapped with collagen, which decreased the fluorescence intensity of type I collagen. After collagenase cleavage, some wrapped-tyrosine could be exposed and thereby the intrinsic fluorescence intensity of collagen increased. By observation and analysis, the influence of collagenase to intrinsic fluorescence of collagen was investigated and elaborated. Furthermore, collagenase cleavage to the special triple helix structure of collagen would result in a slight improvement of collagen thermostability, which was explained by the increasing amount of terminal peptides. These results are helpful and effective for reaction mechanism research related to collagen, which can be observed by fluorescent technology. Meantime, the reaction behaviors of both collagenase and collagenolytic proteases can also be analyzed by fluorescent technology. In conclusion, this research provides a foundation for the further investigation of collagen reactions in different areas, such as medicine, nutrition, food and agriculture.

scholarly journals Fourier transform infrared conformational investigation of type I collagen aged by in vitro induced dehydration and non-enzymatic glycation treatments

2017 ◽  
Vol 90 (1) ◽  
Author(s):  
Maria Grazia Bridelli ◽  
Chiaramaria Stani ◽  
Roberta Bedotti
Keyword(s):  
Fourier Transform ◽  
Protein Structure ◽  
Conformational Changes ◽  
Self Assembly ◽  
Type I Collagen ◽  
Protein Secondary Structure ◽  
Fourier Transform Infrared ◽  
Type I ◽  
Absorption Bands

The two main ageing-inducing events in the collagenous tissues are the water loss and the formation of intermolecular crosslinks based on the reaction of collagen with matrix carbohydrates, following a mechanism known as non-enzymatic-glycation. With the aim to mimic the two deleterious processes for the protein structure, rat-tail collagen was submitted to hydration changes and allowed to interact with two sugars characterized by different reducing properties, D-glucose and D-ribose. Fourier transform infrared (FTIR) spectroscopy was employed to investigate the conformational changes induced in the protein by the two treatments by analyzing the subsequent spectra modifications. FTIR spectra monitored: i) the amplitude and position changes of the two characteristic absorption bands OH stretching and Amide I, in dependence on the humidity level: a significant hysteresis effect in the ν(OH) band (ν~3400 cm–1) amplitude of the protein dehydrated and then rehydrated to the initial relative humidity (aw=0.92- 0.06) may be related to the enhancement of the β-sheet fraction in the protein structure as revealed by the parallel modification in the Amide I band (ν~1650 cm–1); ii) the area of the carbohydrate double band peaking at 1080 cm–1 and 1031 cm–1, associated to the accumulation of the glycation products, depending on the sugar concentration and incubation time. The association of both sugars to collagen only minimally affects the protein secondary structure as revealed by Amide I band Gaussian analysis. The whole set of results suggests hints to hypothesize a self-assembly model for collagen molecules induced by ageing.

Visualization of Flow-Aligned Type I Collagen Self-Assembly in Tunable pH Gradients

Langmuir ◽  
2007 ◽  
Vol 23 (2) ◽  
pp. 357-359 ◽  
Author(s):  
Sarah Köster ◽  
Jennie B. Leach ◽  
Bernd Struth ◽  
Thomas Pfohl ◽  
Joyce Y. Wong
Keyword(s):  
Self Assembly ◽  
Type I Collagen ◽  
Type I ◽  
Ph Gradients

Self-assembly nano-structure of type I collagen adsorbed on Gemini surfactant LB monolayers

2009 ◽  
Vol 70 (1) ◽  
pp. 124-131 ◽  
Author(s):  
Shouhong Xu ◽  
Aiping Liu ◽  
Qibin Chen ◽  
Mingyu Lv ◽  
Masakastu Yonese ◽  
...  
Keyword(s):  
Self Assembly ◽  
Gemini Surfactant ◽  
Type I Collagen ◽  
Type I ◽  
Nano Structure

Microaligned collagen matrices by hydrodynamic focusing: controlling the pH-induced self-assembly

2005 ◽  
Vol 898 ◽  
Author(s):  
Sarah Köester ◽  
Jennie B Leach ◽  
Thomas Pfohl ◽  
Joyce Y Wong
Keyword(s):  
Self Assembly ◽  
Type I Collagen ◽  
Polarized Light ◽  
Type I ◽  
Hydrodynamic Focusing ◽  
Microfluidic Mixing ◽  
Ph Gradients ◽  
The Hierarchical Structure ◽  
Local Ph

AbstractThe hierarchical structure of type I collagen fibrils is a key contributor to the mechanical properties of the extracellular matrix (ECM). It is known that the process of in vitro fibrillogenesis strongly depends on the pH of the collagen solution. To date, there are few methods available for precisely controlling and investigating the dependence of collagen fibril assembly on the local pH. The objective of this work was to create highly defined pH gradients to systematically determine the effects of local pH on microscale collagen fibrillogenesis and alignment. We use a microfluidic mixing device to create a diffusion controlled pH gradient, which in turn initiates the self-assembly and concurrent flow-alignment of soluble collagen. Finite element method simulations of the hydrodynamic and diffusive phenomena are used to calculate the local concentrations of the components involved in the reaction. We develop a model to analytically calculate the local pH in the microfluidic device from these concentrations. A comparison with the experimental results from polarized light microscopy are in good agreement with the simulations.

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