scholarly journals Structure-property-function relationships in triple-helical collagen hydrogels

2012 ◽  
Vol 1498 ◽  
pp. 145-150 ◽  
Author(s):  
Giuseppe Tronci ◽  
Amanda Doyle ◽  
Stephen J. Russell ◽  
David J. Wood
Keyword(s):  
Triple Helix ◽  
Type I Collagen ◽  
Molecular Organization ◽  
Type I ◽  
Tissue Formation ◽  
Structure Property ◽  
Mineralized Tissue ◽  
Mineral Deposition ◽  
Collagen Hydrogels ◽  
Macroscopic Properties

ABSTRACTIn order to establish defined biomimetic systems, type I collagen was functionalised with 1,3-Phenylenediacetic acid (Ph) as aromatic, bifunctional segment. Following investigation on molecular organization and macroscopic properties, material functionalities, i.e. degradability and bioactivity, were addressed, aiming at elucidating the potential of this collagen system as mineralization template. Functionalised collagen hydrogels demonstrated a preserved triple helix conformation. Decreased swelling ratio and increased thermo-mechanical properties were observed in comparison to state-of-the-art carbodiimide (EDC)-crosslinked collagen controls. Ph-crosslinked samples displayed no optical damage and only a slight mass decrease (∼ 4 wt.-%) following 1-week incubation in simulated body fluid (SBF), while nearly 50 wt.-% degradation was observed in EDC-crosslinked collagen. SEM/EDS revealed amorphous mineral deposition, whereby increased calcium phosphate ratio was suggested in hydrogels with increased Ph content. This investigation provides valuable insights for the synthesis of triple helical collagen materials with enhanced macroscopic properties and controlled degradation. In light of these features, this system will be applied for the design of tissue-like scaffolds for mineralized tissue formation.

scholarly journals Multi-scale mechanical characterization of highly swollen photo-activated collagen hydrogels

2015 ◽  
Vol 12 (102) ◽  
pp. 20141079 ◽  
Author(s):  
Giuseppe Tronci ◽  
Colin A. Grant ◽  
Neil H. Thomson ◽  
Stephen J. Russell ◽  
David J. Wood
Keyword(s):  
Mechanical Properties ◽  
Type I Collagen ◽  
Wound Care ◽  
Wound Dressings ◽  
Type I ◽  
Structure Property ◽  
Multi Scale ◽  
Macro Scale ◽  
Collagen Hydrogels ◽  
Tunable Mechanical Properties

Biological hydrogels have been increasingly sought after as wound dressings or scaffolds for regenerative medicine, owing to their inherent biofunctionality in biological environments. Especially in moist wound healing, the ideal material should absorb large amounts of wound exudate while remaining mechanically competent in situ . Despite their large hydration, however, current biological hydrogels still leave much to be desired in terms of mechanical properties in physiological conditions. To address this challenge, a multi-scale approach is presented for the synthetic design of cyto-compatible collagen hydrogels with tunable mechanical properties (from the nano- up to the macro-scale), uniquely high swelling ratios and retained (more than 70%) triple helical features. Type I collagen was covalently functionalized with three different monomers, i.e. 4-vinylbenzyl chloride, glycidyl methacrylate and methacrylic anhydride, respectively. Backbone rigidity, hydrogen-bonding capability and degree of functionalization ( F : 16 ± 12–91 ± 7 mol%) of introduced moieties governed the structure–property relationships in resulting collagen networks, so that the swelling ratio ( SR : 707 ± 51–1996 ± 182 wt%), bulk compressive modulus ( E c : 30 ± 7–168 ± 40 kPa) and atomic force microscopy elastic modulus ( E AFM : 16 ± 2–387 ± 66 kPa) were readily adjusted. Because of their remarkably high swelling and mechanical properties, these tunable collagen hydrogels may be further exploited for the design of advanced dressings for chronic wound care.

scholarly journals Contrasting Local and Macroscopic Effects of Collagen Hydroxylation

2021 ◽  
Vol 22 (16) ◽  
pp. 9068
Author(s):  
Sameer Varma ◽  
Joseph P. R. O. Orgel ◽  
Jay D. Schieber
Keyword(s):  
Molecular Dynamics ◽  
Hydrogen Bonding ◽  
Local Structure ◽  
Triple Helix ◽  
Type I Collagen ◽  
Chemical Change ◽  
Fibrillar Structure ◽  
Minor Effect ◽  
Type I ◽  
Macroscopic Properties

Collagen is heavily hydroxylated. Experiments show that proline hydroxylation is important to triple helix (monomer) stability, fibril assembly, and interaction of fibrils with other molecules. Nevertheless, experiments also show that even without hydroxylation, type I collagen does assemble into its native D-banded fibrillar structure. This raises two questions. Firstly, even though hydroxylation removal marginally affects macroscopic structure, how does such an extensive chemical change, which is expected to substantially reduce hydrogen bonding capacity, affect local structure? Secondly, how does such a chemical perturbation, which is expected to substantially decrease electrostatic attraction between monomers, affect collagen’s mechanical properties? To address these issues, we conduct a benchmarked molecular dynamics study of rat type I fibrils in the presence and absence of hydroxylation. Our simulations reproduce the experimental observation that hydroxylation removal has a minimal effect on collagen’s D-band length. We also find that the gap-overlap ratio, monomer width and monomer length are minimally affected. Surprisingly, we find that de-hydroxylation also has a minor effect on the fibril’s Young’s modulus, and elastic stress build up is also accompanied by tightening of triple-helix windings. In terms of local structure, de-hydroxylation does result in a substantial drop (23%) in inter-monomer hydrogen bonding. However, at the same time, the local structures and inter-monomer hydrogen bonding networks of non-hydroxylated amino acids are also affected. It seems that it is this intrinsic plasticity in inter-monomer interactions that preclude fibrils from undergoing any large changes in macroscopic properties. Nevertheless, changes in local structure can be expected to directly impact collagen’s interaction with extra-cellular matrix proteins. In general, this study highlights a key challenge in tissue engineering and medicine related to mapping collagen chemistry to macroscopic properties but suggests a path forward to address it using molecular dynamics simulations.

scholarly journals Comprehensive Assessment of Nile Tilapia Skin (Oreochromis niloticus) Collagen Hydrogels for Wound Dressings

Marine Drugs ◽  
2020 ◽  
Vol 18 (4) ◽  
pp. 178 ◽  
Author(s):  
Baosheng Ge ◽  
Haonan Wang ◽  
Jie Li ◽  
Hengheng Liu ◽  
Yonghao Yin ◽  
...  
Keyword(s):  
Wound Dressing ◽  
Type I Collagen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Wound Dressings ◽  
Type I ◽  
Rheological Characterization ◽  
Scanning Calorimetry ◽  
Soluble Collagen ◽  
Collagen Hydrogels

Collagen plays an important role in the formation of extracellular matrix (ECM) and development/migration of cells and tissues. Here we report the preparation of collagen and collagen hydrogel from the skin of tilapia and an evaluation of their potential as a wound dressing for the treatment of refractory wounds. The acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were extracted and characterized using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), differential scanning calorimetry (DSC), circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR) analysis. Both ASC and PSC belong to type I collagen and have a complete triple helix structure, but PSC shows lower molecular weight and thermal stability, and has the inherent low antigenicity. Therefore, PSC was selected to prepare biomedical hydrogels using its self-aggregating properties. Rheological characterization showed that the mechanical strength of the hydrogels increased as the PSC content increased. Scanning electron microscope (SEM) analysis indicated that hydrogels could form a regular network structure at a suitable PSC content. Cytotoxicity experiments confirmed that hydrogels with different PSC content showed no significant toxicity to fibroblasts. Skin repair experiments and pathological analysis showed that the collagen hydrogels wound dressing could significantly accelerate the healing of deep second-degree burn wounds and the generation of new skin appendages, which can be used for treatment of various refractory wounds.

scholarly journals Structural Heterogeneity of Type I Collagen Triple Helix and Its Role in Osteogenesis Imperfecta

2007 ◽  
Vol 283 (8) ◽  
pp. 4787-4798 ◽  
Author(s):  
Elena Makareeva ◽  
Edward L. Mertz ◽  
Natalia V. Kuznetsova ◽  
Mary B. Sutter ◽  
Angela M. DeRidder ◽  
...  
Keyword(s):  
Osteogenesis Imperfecta ◽  
Triple Helix ◽  
Type I Collagen ◽  
Structural Heterogeneity ◽  
Type I ◽  
Collagen Triple Helix

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.

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