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: 30 September 2021.

Special Issue Editor

Dr. Andreas Stylianou
E-Mail Website
Guest Editor
Department of Mechanical and Manufacturing Engineering, Faculty of Engineering/University of 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

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Materials is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2000 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

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 (3 papers)

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Research

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Open AccessArticle
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 1 | Viewed by 537
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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Open AccessArticle
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 6 | Viewed by 835
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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Open AccessReview
Collagen Based Materials in Cosmetic Applications: A Review
Materials 2020, 13(19), 4217; https://doi.org/10.3390/ma13194217 - 23 Sep 2020
Cited by 3 | Viewed by 1151
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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