Special Issue "Collagens, Collagen-Based and Collagen-Mimetic Biomaterials: Preparation, Characterization and Applications"

A special issue of Materials (ISSN 1996-1944).

Deadline for manuscript submissions: 20 May 2022 | Viewed by 7433

Special Issue Editor

Dr. Andreas Stylianou
E-Mail Website
Guest Editor
Department of Mechanical and Manufacturing Engineering, Faculty of Engineering, University of Cyprus, Nicosia, Cyprus
Interests: atomic force microscopy—AFM; nano-biomaterials; collagen (collagen-based biomaterials, collagen-related pathological conditions, collagen characterization) cell/tissue nanomechanical properties; tumor microenvironment—TME—components; cell–biomaterial interactions; interactions between biological tissues and laser/optical radiation; novel medical imaging techniques and science ethics/bioethics

Special Issue Information

Dear Colleagues,

Collagens are the major proteins in the extracellular matrix (ECM) and comprise almost 30% of the total cell proteins in mammals. The superfamily of collagen in vertebrates includes over 50 collagens and collagen-like proteins that play a key role in tissue homeostasis, and they have also been implicated in a wide range of pathological conditions. The numerous biomaterials, collagen-based, and collagen-mimetic biomaterials are of great interest, because they present unique properties and have a wide range of applications in the fields of biomaterials, tissue engineering, and biomedicine, including implants, scaffolds, hydrogels, and coatings. To that regard, novel techniques and methods are emerging for the design, characterization, and development of innovative and advanced biomaterials in order to provide improved performance for specific applications.

The present Special Issue welcomes contributions in the form of full articles, short communications, or review articles on topics related to the design, synthesis, characterization, surface modification, and processing of collagen-based and collagen-mimetic biomaterials for use in different biomedical applications.

Dr. Andreas Stylianou
Guest Editor

Manuscript Submission Information

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Keywords

  • Collagen
  • Collagen-based biomaterials
  • Collagen-mimetic biomaterials
  • Collagen characteristics (fibers/fibrils, D-band periodicity, orientation, diameter, etc.)
  • Scaffolds
  • Implants
  • Hydrogels
  • Three-dimensional gels
  • Nanomaterials
  • Nanofibers
  • Electrospinning
  • Coatings
  • Tissue engineering
  • Biocompatibility
  • Cell–materials interactions
  • Material characterization
  • Extracellular matrices
  • Biomaterials surface characterization techniques
  • Biomaterials imaging techniques
  • Collagen-related diseases (fibrosis, desmoplasia/cancer, osteoarthritis, etc.)

Published Papers (6 papers)

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Research

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Article
Characterization of Five Collagenous Biomaterials by SEM Observations, TG-DTA, Collagenase Dissolution Tests and Subcutaneous Implantation Tests
Materials 2022, 15(3), 1155; https://doi.org/10.3390/ma15031155 - 02 Feb 2022
Viewed by 414
Abstract
Collagenous biomaterials that are clinically applied in dentistry have dermis-type and membrane-type, both of which are materials for promoting bone and soft tissue formation. The properties of materials supplied with different types could affect their biodegradation periods. The purpose of this study was [...] Read more.
Collagenous biomaterials that are clinically applied in dentistry have dermis-type and membrane-type, both of which are materials for promoting bone and soft tissue formation. The properties of materials supplied with different types could affect their biodegradation periods. The purpose of this study was to characterize five of these products by four different methods: scanning electron microscopy (SEM) observation, thermogravimetry-differential thermal analysis (TG-DTA), 0.01 wt% collagenase dissolution test, and subcutaneous implantation test in vivo. SEM micrographs revealed that both dermis and membranous materials were fibrous and porous. The membranous materials had higher specific derivative thermal gravimetry (DTG) peak temperatures in TG-DTA at around 320 °C, longer collagenase dissolution time ranging from about 300 to 500 min, and more longevity in mice exceeding 9 weeks than the dermis materials. There existed a correlation between the peak temperature in TG-DTA and the collagenase dissolution time. It was considered that higher cross-link degree among collagen fibrils of the membrane-type collagenous materials might account for these phenomena. The experimental protocol and numerical results obtained could be helpful for selection and future development of fibrous collagenous biomaterials in clinical use. Full article
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Article
The Influence of UV Light on Rheological Properties of Collagen Extracted from Silver Carp Skin
Materials 2020, 13(19), 4453; https://doi.org/10.3390/ma13194453 - 08 Oct 2020
Cited by 7 | Viewed by 915
Abstract
Acid soluble collagen (ASC) was extracted from Silver Carp fish skin. Collagen was dissolved in acetic acid at varying concentrations and its rheological properties were studied. Steady shear flow properties of collagen solutions at concentrations of 5 and 10 mg/mL were characterized using [...] Read more.
Acid soluble collagen (ASC) was extracted from Silver Carp fish skin. Collagen was dissolved in acetic acid at varying concentrations and its rheological properties were studied. Steady shear flow properties of collagen solutions at concentrations of 5 and 10 mg/mL were characterized using rheometry at 20 °C. Collagen solutions were irradiated with UV light (wavelength 254 nm) for up to 2 h and rheological properties were measured. All the collagen solutions showed a shear-thinning flow behavior. A constant viscosity region was observed after 1 h of UV irradiation, which showed that collagen molecules were fully denatured. A short treatment with collagen solution by UV (ultraviolet) light led to an increase in viscosity; however, the denaturation temperature of UV-irradiated collagen decreased. Depending on the time of UV treatment, collagen extracted from Silver Carp fish skin may undergo physical crosslinking or photodegradation. Physically crosslinked collagen may find applications in functional food, cosmetic, biomedical, and pharmaceutical industries. Full article
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Article
Tissue Integration and Degradation of a Porous Collagen-Based Scaffold Used for Soft Tissue Augmentation
Materials 2020, 13(10), 2420; https://doi.org/10.3390/ma13102420 - 25 May 2020
Cited by 13 | Viewed by 1318
Abstract
Collagen-based scaffolds hold great potential for tissue engineering, since they closely mimic the extracellular matrix. We investigated tissue integration of an engineered porous collagen-elastin scaffold developed for soft tissue augmentation. After implantation in maxillary submucosal pouches in 6 canines, cell invasion (vimentin), extracellular [...] Read more.
Collagen-based scaffolds hold great potential for tissue engineering, since they closely mimic the extracellular matrix. We investigated tissue integration of an engineered porous collagen-elastin scaffold developed for soft tissue augmentation. After implantation in maxillary submucosal pouches in 6 canines, cell invasion (vimentin), extracellular matrix deposition (collagen type I) and scaffold degradation (cathepsin k, tartrate-resistant acid phosphatase (TRAP), CD86) were (immuno)-histochemically evaluated. Invasion of vimentin+ cells (scattered and blood vessels) and collagen type I deposition within the pores started at 7 days. At 15 and 30 days, vimentin+ cells were still numerous and collagen type I increasingly filled the pores. Scaffold degradation was characterized by collagen loss mainly occurring around 15 days, a time point when medium-sized multinucleated cells peaked at the scaffold margin with simultaneous labeling for cathepsin k, TRAP, and CD86. Elastin was more resistant to degradation and persisted up to 90 days in form of packages well-integrated in the newly formed soft connective tissue. In conclusion, this collagen-based scaffold maintained long-enough volume stability to allow an influx of blood vessels and vimentin+ fibroblasts producing collagen type I, that filled the scaffold pores before major biomaterial degradation and collapse occurred. Cathepsin k, TRAP and CD86 appear to be involved in scaffold degradation. Full article
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Review

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Review
Atomic Force Microscopy Nanoindentation Method on Collagen Fibrils
Materials 2022, 15(7), 2477; https://doi.org/10.3390/ma15072477 - 27 Mar 2022
Viewed by 488
Abstract
Atomic Force Microscopy nanoindentation method is a powerful technique that can be used for the nano-mechanical characterization of bio-samples. Significant scientific efforts have been performed during the last two decades to accurately determine the Young’s modulus of collagen fibrils at the nanoscale, as [...] Read more.
Atomic Force Microscopy nanoindentation method is a powerful technique that can be used for the nano-mechanical characterization of bio-samples. Significant scientific efforts have been performed during the last two decades to accurately determine the Young’s modulus of collagen fibrils at the nanoscale, as it has been proven that mechanical alterations of collagen are related to various pathological conditions. Different contact mechanics models have been proposed for processing the force–indentation data based on assumptions regarding the shape of the indenter and collagen fibrils and on the elastic or elastic–plastic contact assumption. However, the results reported in the literature do not always agree; for example, the Young’s modulus values for dry collagen fibrils expand from 0.9 to 11.5 GPa. The most significant parameters for the broad range of values are related to the heterogeneous structure of the fibrils, the water content within the fibrils, the data processing errors, and the uncertainties in the calibration of the probe. An extensive discussion regarding the models arising from contact mechanics and the results provided in the literature is presented, while new approaches with respect to future research are proposed. Full article
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Review
Assessing Collagen D-Band Periodicity with Atomic Force Microscopy
Materials 2022, 15(4), 1608; https://doi.org/10.3390/ma15041608 - 21 Feb 2022
Viewed by 506
Abstract
The collagen superfamily includes more than fifty collagen and/or collagen-like proteins with fibril-forming collagen type I being the most abundant protein within the extracellular matrix. Collagen type I plays a crucial role in a variety of functions, it has been associated with many [...] Read more.
The collagen superfamily includes more than fifty collagen and/or collagen-like proteins with fibril-forming collagen type I being the most abundant protein within the extracellular matrix. Collagen type I plays a crucial role in a variety of functions, it has been associated with many pathological conditions and it is widely used due to its unique properties. One unique nano-scale characteristic of natural occurring collagen type I fibers is the so-called D-band periodicity, which has been associated with collagen natural structure and properties, while it seems to play a crucial role in the interactions between cells and collagen and in various pathological conditions. An accurate characterization of the surface and structure of collagen fibers, including D-band periodicity, on collagen-based tissues and/or (nano-)biomaterials can be achieved by Atomic Force Microscopy (AFM). AFM is a scanning probe microscope and is among the few techniques that can assess D-band periodicity. This review covers issues related to collagen and collagen D-band periodicity and the use of AFM for studying them. Through a systematic search in databases (PubMed and Scopus) relevant articles were identified. The study of these articles demonstrated that AFM can offer novel information concerning D-band periodicity. This study highlights the importance of studying collagen D-band periodicity and proves that AFM is a powerful tool for investigating a number of different properties related to collagen D-band periodicity. Full article
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Review
Collagen Based Materials in Cosmetic Applications: A Review
Materials 2020, 13(19), 4217; https://doi.org/10.3390/ma13194217 - 23 Sep 2020
Cited by 21 | Viewed by 3122
Abstract
This review provides a report on properties and recent advances in the application of collagen in cosmetics. Collagen is a structural protein found in animal organisms where it provides for the fundamental structural support. Most commonly it is extracted from mammalian and fish [...] Read more.
This review provides a report on properties and recent advances in the application of collagen in cosmetics. Collagen is a structural protein found in animal organisms where it provides for the fundamental structural support. Most commonly it is extracted from mammalian and fish skin. Collagen has attracted significant academic interest as well as the attention of the cosmetic industry due to its interesting properties that include being a natural humectant and moisturizer for the skin. This review paper covers the biosynthesis of collagen, the sources of collagen used in the cosmetic industry, and the role played by this protein in cosmetics. Future aspects regarding applications of collagen-based materials in cosmetics have also been mentioned. Full article
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