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Special Issue "Collagen from Marine Biological Source and Medical Applications"

A special issue of Marine Drugs (ISSN 1660-3397).

Deadline for manuscript submissions: closed (30 November 2018)

Special Issue Editors

Guest Editor
Dr. Azizur Rahman

Department of Physical & Environmental Sciences, University of Toronto, Canada
Website | E-Mail
Interests: marine proteins; soft corals; marine collagen; marine chitin; marine polysaccharides; drug discovery; biomineralization; biomaterials; marine invertebrates; marine algae; proteomics; marine Biotechnology
Guest Editor
Dr. Tiago H. Silva

3B's Research Group in Biomaterials, Biodegradables and Biomimetics, University of Minho, Guimarães, Portugal
Website | E-Mail
Interests: Marine biomaterials; valorization of marine resources and by-products; marine biotechnology; Bioinspired materials; tissue engineering

Special Issue Information

Dear Colleagues,

Collagen is the main fibrous structural protein in the extracellular matrix and connective tissue of animals. It is a primary building block of bones, tendons, skin, hair, nails, cartilage, and all joints in the body. It is also considered a "glue" that holds the body together. The production of collagen begins to slow down and cell structures start losing their strength as we get older. Supplementing with collagen is a vital way to help our body revive and stay youthful. Recently, collagen-based biomedical materials have developed important and clinically effective materials that have gained wide acceptance. However, collagen extraction from land animal source is complex, time consuming and expensive. Hence, marine sources have started to be researched and have been found to be the most convenient and safest sources for obtaining collagen. Another reason for favouring this source is due to the concern over adverse inflammatory and immunologic response and prevalence of various diseases among land animals which causes health complications.

Marine source also has plenty of advantages over the land animal sources such as: (1) High content of collagen; (2) environment friendly; (3) presence of biological contaminants and toxins almost negligible; (4) low inflammatory response; (5) greater absorption due to low molecular weight; (6) less significant religious and ethical constrains; (7) minor regulatory and quality control problems; (8) metabolically compatible, and much more. This source includes the use of marine invertebrates and vertebrates, such as sponges, coralline red algae, sea urchin, octopus, squid, jellyfish, cuttlefish, star fish, sea anemone, and prawn. Therefore, a huge source of marine collagen is expected to make a great contribution to marine biotechnology products and medical applications.

As Guest Editors of this Special Issue of Marine Drugs, We invite you to submit recent advances in all the aspects of marine collagen, including original work or reviews and new innovations on the biological sources and their promising applications in medical and related fields.

Dr. Azizur Rahman
Dr. Tiago H. Silva
Guest Editors

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. Marine Drugs is an international peer-reviewed open access monthly 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

  • Chitin

  • Marine skeletal proteins

  • Biominerals

  • Marine biotechnology

  • Marine Biomaterials

  • Corals

  • Sponges

  • Biomedical applications

  • Marine algae

  • Proteomics

Published Papers (18 papers)

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Open AccessArticle
Physicochemical and Biocompatibility Properties of Type I Collagen from the Skin of Nile Tilapia (Oreochromis niloticus) for Biomedical Applications
Mar. Drugs 2019, 17(3), 137; https://doi.org/10.3390/md17030137
Received: 29 December 2018 / Revised: 16 February 2019 / Accepted: 20 February 2019 / Published: 26 February 2019
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Abstract
The aim of this study is to investigate the physicochemical properties, biosafety, and biocompatibility of the collagen extract from the skin of Nile tilapia, and evaluate its use as a potential material for biomedical applications. Two extraction methods were used to obtain acid-soluble [...] Read more.
The aim of this study is to investigate the physicochemical properties, biosafety, and biocompatibility of the collagen extract from the skin of Nile tilapia, and evaluate its use as a potential material for biomedical applications. Two extraction methods were used to obtain acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from tilapia skin. Amino acid composition, FTIR, and SDS-PAGE results showed that ASC and PSC were type I collagen. The molecular form of ASC and PSC is (α1)2α2. The FTIR spectra of ASC and PSC were similar, and the characteristic peaks corresponding to amide A, amide B, amide I, amide II, and amide III were 3323 cm−1, 2931 cm−1, 1677 cm−1, 1546 cm−1, and 1242 cm−1, respectively. Denaturation temperatures (Td) were 36.1 °C and 34.4 °C, respectively. SEM images showed the loose and porous structure of collagen, indicting its physical foundation for use in applications of biomedical materials. Negative results were obtained in an endotoxin test. Proliferation rates of osteoblastic (MC3T3E1) cells and fibroblast (L929) cells from mouse and human umbilical vein endothelial cells (HUVEC) were increased in the collagen-treated group compared with the controls. Furthermore, the acute systemic toxicity test showed no acute systemic toxicity of the ASC and PSC collagen sponges. These findings indicated that the collagen from Nile tilapia skin is highly biocompatible in nature and could be used as a suitable biomedical material. Full article
(This article belongs to the Special Issue Collagen from Marine Biological Source and Medical Applications)
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Open AccessArticle
Collagen Extraction Optimization from the Skin of the Small-Spotted Catshark (S. canicula) by Response Surface Methodology
Mar. Drugs 2019, 17(1), 40; https://doi.org/10.3390/md17010040
Received: 29 November 2018 / Revised: 26 December 2018 / Accepted: 27 December 2018 / Published: 9 January 2019
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Abstract
The small-spotted catshark is one of the most abundant elasmobranchs in the Northeastern Atlantic Ocean. Although its landings are devoted for human consumption, in general this species has low commercial value with high discard rates, reaching 100% in some European fisheries. The reduction [...] Read more.
The small-spotted catshark is one of the most abundant elasmobranchs in the Northeastern Atlantic Ocean. Although its landings are devoted for human consumption, in general this species has low commercial value with high discard rates, reaching 100% in some European fisheries. The reduction of post-harvest losses (discards and by-products) by promotion of a full use of fishing captures is one of the main goals of EU fishing policies. As marine collagens are increasingly used as alternatives to mammalian collagens for cosmetics, tissue engineering, etc., fish skins represent an excellent and abundant source for obtaining this biomolecule. The aim of this study was to analyze the influence of chemical treatment concentration, temperature and time on the extractability of skin collagen from this species. Two experimental designs, one for each of the main stages of the process, were performed by means of Response Surface Methodology (RSM). The combined effect of NaOH concentration, time and temperature on the amount of collagen recovered in the first stage of the collagen extraction procedure was studied. Then, skins treated under optimal NaOH conditions were subjected to a second experimental design, to study the combined effect of AcOH concentration, time and temperature on the collagen recovery by means of yield, amino acid content and SDS-PAGE characterization. Values of independent variables maximizing collagen recovery were 4 °C, 2 h and 0.1 M NaOH (pre-treatment) and 25 °C, 34 h and 1 M AcOH (collagen extraction). Full article
(This article belongs to the Special Issue Collagen from Marine Biological Source and Medical Applications)
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Open AccessArticle
Fish Collagen Surgical Compress Repairing Characteristics on Wound Healing Process In Vivo
Mar. Drugs 2019, 17(1), 33; https://doi.org/10.3390/md17010033
Received: 12 October 2018 / Revised: 16 November 2018 / Accepted: 20 November 2018 / Published: 8 January 2019
Cited by 2 | PDF Full-text (3385 KB) | HTML Full-text | XML Full-text
Abstract
The development of biomaterials with the potential to accelerate wound healing is a great challenge in biomedicine. In this study, four types of samples including pepsin soluble collagen sponge (PCS), acid soluble collagen sponge (ACS), bovine collagen electrospun I (BCE I) and bovine [...] Read more.
The development of biomaterials with the potential to accelerate wound healing is a great challenge in biomedicine. In this study, four types of samples including pepsin soluble collagen sponge (PCS), acid soluble collagen sponge (ACS), bovine collagen electrospun I (BCE I) and bovine collagen electrospun II (BCE II) were used as wound dressing materials. We showed that the PCS, ACS, BCE I and BCE II treated rats increased the percentage of wound contraction, reduced the inflammatory infiltration, and accelerated the epithelization and healing. PCS, ACS, BCE I, and BCE II significantly enhanced the total protein and hydroxyproline level in rats. ACS could induce more fibroblasts proliferation and differentiation than PCS, however, both PCS and ACS had a lower effect than BCE I and BCE II. PCS, ACS, BCE I, and BCE II could regulate deposition of collagen, which led to excellent alignment in the wound healing process. There were similar effects on inducing the level of cytokines including EGF, FGF, and vascular endothelial marker CD31 among these four groups. Accordingly, this study disclosed that collagens (PCS and ACS) from tilapia skin and bovine collagen electrospun (BCE I and BCE II) have significant bioactivity and could accelerate wound healing rapidly and effectively in rat model. Full article
(This article belongs to the Special Issue Collagen from Marine Biological Source and Medical Applications)
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Open AccessArticle
Development of an Integrated Mariculture for the Collagen-Rich Sponge Chondrosia reniformis
Mar. Drugs 2019, 17(1), 29; https://doi.org/10.3390/md17010029
Received: 29 November 2018 / Revised: 26 December 2018 / Accepted: 27 December 2018 / Published: 5 January 2019
Cited by 1 | PDF Full-text (3430 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
In this study, novel methods were tested to culture the collagen-rich sponge Chondrosia reniformis Nardo, 1847 (Demospongiae, Chondrosiida, Chondrosiidae) in the proximity of floating fish cages. In a trial series, survival and growth of cultured explants were monitored near a polluted fish farm [...] Read more.
In this study, novel methods were tested to culture the collagen-rich sponge Chondrosia reniformis Nardo, 1847 (Demospongiae, Chondrosiida, Chondrosiidae) in the proximity of floating fish cages. In a trial series, survival and growth of cultured explants were monitored near a polluted fish farm and a pristine control site. Attachment methods, plate materials, and plate orientation were compared. In a first trial, chicken wire-covered polyvinyl chloride (PVC) was found to be the most suitable substrate for C. reniformis (100% survival). During a second trial, survival on chicken wire-covered PVC, after six months, was 79% and 63% for polluted and pristine environments, respectively. Net growth was obtained only on culture plates that were oriented away from direct sunlight (39% increase in six months), whereas sponges decreased in size when sun-exposed. Chicken wire caused pressure on explants and it resulted in unwanted epibiont growth and was therefore considered to be unsuitable for long-term culture. In a final trial, sponges were glued to PVC plates and cultured for 13 months oriented away from direct sunlight. Both survival and growth were higher at the polluted site (86% survival and 170% growth) than at the pristine site (39% survival and 79% growth). These results represent a first successful step towards production of sponge collagen in integrated aquacultures. Full article
(This article belongs to the Special Issue Collagen from Marine Biological Source and Medical Applications)
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Open AccessArticle
Electrodialysis Extraction of Pufferfish Skin (Takifugu flavidus): A Promising Source of Collagen
Mar. Drugs 2019, 17(1), 25; https://doi.org/10.3390/md17010025
Received: 28 November 2018 / Revised: 12 December 2018 / Accepted: 27 December 2018 / Published: 4 January 2019
Cited by 1 | PDF Full-text (1757 KB) | HTML Full-text | XML Full-text
Abstract
Collagen is widely used in drugs, biomaterials, foods, and cosmetics. By-products of the fishing industry are rich sources of collagen, which can be used as an alternative to collagen traditionally harvested from land mammals. However, commercial applications of fish-based collagen are limited by [...] Read more.
Collagen is widely used in drugs, biomaterials, foods, and cosmetics. By-products of the fishing industry are rich sources of collagen, which can be used as an alternative to collagen traditionally harvested from land mammals. However, commercial applications of fish-based collagen are limited by the low efficiency, low productivity, and low sustainability of the extraction process. This study applied a new technique (electrodialysis) for the extraction of Takifugu flavidus skin collagen. We found electrodialysis to have better economic and environmental outcomes than traditional dialysis as it significantly reduced the purification time and wastewater (~95%) while maintaining high extraction yield (67.3 ± 1.3 g/100 g dry weight, p < 0.05). SDS-PAGE, amino acid composition analysis, and spectrophotometric characterization indicated that electrodialysis treatment retained the physicochemical properties of T. flavidus collagen. Heavy metals and tetrodotoxin analyses indicated the safety of T. flavidus collagen. Notably, the collagen had similar thermal stability to calf skin collagen, with the maximum transition temperature and denaturation temperature of 41.8 ± 0.35 and 28.4 ± 2.5 °C, respectively. All evidence suggests that electrodialysis is a promising technique for extracting collagen in the fishing industry and that T. flavidus skin collagen could serve as an alternative source of collagen to meet the increasing demand from consumers. Full article
(This article belongs to the Special Issue Collagen from Marine Biological Source and Medical Applications)
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Open AccessFeature PaperArticle
Evaluation of the Potential of Collagen from Codfish Skin as a Biomaterial for Biomedical Applications
Mar. Drugs 2018, 16(12), 495; https://doi.org/10.3390/md16120495
Received: 6 November 2018 / Revised: 30 November 2018 / Accepted: 5 December 2018 / Published: 8 December 2018
Cited by 2 | PDF Full-text (1471 KB) | HTML Full-text | XML Full-text
Abstract
Collagen is one of the most widely used biomaterials, not only due its biocompatibility, biodegradability and weak antigenic potential, but also due to its role in the structure and function of tissues. Searching for alternative collagen sources, the aim of this study was [...] Read more.
Collagen is one of the most widely used biomaterials, not only due its biocompatibility, biodegradability and weak antigenic potential, but also due to its role in the structure and function of tissues. Searching for alternative collagen sources, the aim of this study was to extract collagen from the skin of codfish, previously obtained as a by-product of fish industrial plants, and characterize it regarding its use as a biomaterial for biomedical application, according to American Society for Testing and Materials (ASTM) Guidelines. Collagen type I with a high degree of purity was obtained through acid-extraction, as confirmed by colorimetric assays, SDS-PAGE and amino acid composition. Thermal analysis revealed a denaturing temperature around 16 °C. Moreover, collagen showed a concentration-dependent effect in metabolism and on cell adhesion of lung fibroblast MRC-5 cells. In conclusion, this study shows that collagen can be obtained from marine-origin sources, while preserving its bioactivity, supporting its use in biomedical applications. Full article
(This article belongs to the Special Issue Collagen from Marine Biological Source and Medical Applications)
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Open AccessArticle
Effects of Composite Supplement Containing Collagen Peptide and Ornithine on Skin Conditions and Plasma IGF-1 Levels—A Randomized, Double-Blind, Placebo-Controlled Trial
Mar. Drugs 2018, 16(12), 482; https://doi.org/10.3390/md16120482
Received: 31 October 2018 / Revised: 28 November 2018 / Accepted: 29 November 2018 / Published: 3 December 2018
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Abstract
Aging-associated changes of skin conditions are a major concern for maintaining quality of life. Therefore, the improvement of skin conditions by dietary supplementation is a topic of public interest. In this study, we hypothesized that a composite supplement containing fish derived-collagen peptide and [...] Read more.
Aging-associated changes of skin conditions are a major concern for maintaining quality of life. Therefore, the improvement of skin conditions by dietary supplementation is a topic of public interest. In this study, we hypothesized that a composite supplement containing fish derived-collagen peptide and ornithine (CPO) could improve skin conditions by increasing plasma growth hormone and/or insulin-like growth factor-1 (IGF-1) levels. Twenty-two healthy Japanese participants were enrolled in an 8-week double-blind placebo-controlled pilot study. They were assigned to either a CPO group, who were supplemented with a drink containing CPO, or an identical placebo group. We examined skin conditions including elasticity and transepidermal water loss (TEWL), as well as plasma growth hormone and IGF-1 levels. Skin elasticity and TEWL were significantly improved in the CPO group compared with the placebo group. Furthermore, only the CPO group showed increased plasma IGF-1 levels after 8 weeks of supplementation compared with the baseline. Our results might suggest the novel possibility for the use of CPO to improve skin conditions by increasing plasma IGF-1 levels. Full article
(This article belongs to the Special Issue Collagen from Marine Biological Source and Medical Applications)
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Open AccessArticle
Evaluation of Differentiated Bone Cells Proliferation by Blue Shark Skin Collagen via Biochemical for Bone Tissue Engineering
Mar. Drugs 2018, 16(10), 350; https://doi.org/10.3390/md16100350
Received: 22 August 2018 / Revised: 7 September 2018 / Accepted: 17 September 2018 / Published: 25 September 2018
Cited by 4 | PDF Full-text (4116 KB) | HTML Full-text | XML Full-text
Abstract
Collagen from a marine resource is believed to have more potential activity in bone tissue engineering and their bioactivity depends on biochemical and structural properties. Considering the above concept, pepsin soluble collagen (PSC) and acid soluble collagen (ASC) from blue shark (Prionace [...] Read more.
Collagen from a marine resource is believed to have more potential activity in bone tissue engineering and their bioactivity depends on biochemical and structural properties. Considering the above concept, pepsin soluble collagen (PSC) and acid soluble collagen (ASC) from blue shark (Prionace glauca) skin were extracted and its biochemical and osteogenic properties were investigated. The hydroxyproline content was higher in PSC than ASC and the purified collagens contained three distinct bands α1, α2, and β dimer. The purity of collagen was confirmed by the RP-HPLC profile and the thermogravimetric data showed a two-step thermal degradation pattern. ASC had a sharp decline in viscosity at 20–30 °C. Scanning electron microscope (SEM) images revealed the fibrillar network structure of collagens. Proliferation rates of the differentiated mouse bone marrow-mesenchymal stem (dMBMS) and differentiated osteoblastic (dMC3T3E1) cells were increased in collagen treated groups rather than the controls and the effect was dose-dependent, which was further supported by higher osteogenic protein and mRNA expression in collagen treated bone cells. Among two collagens, PSC had significantly increased dMBMS cell proliferation and this was materialized through increasing RUNX2 and collagen-I expression in bone cells. Accordingly, the collagens from blue shark skin with excellent biochemical and osteogenic properties could be a suitable biomaterial for therapeutic application. Full article
(This article belongs to the Special Issue Collagen from Marine Biological Source and Medical Applications)
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Open AccessArticle
Collagen from Cartilaginous Fish By-Products for a Potential Application in Bioactive Film Composite
Mar. Drugs 2018, 16(6), 211; https://doi.org/10.3390/md16060211
Received: 2 May 2018 / Revised: 17 May 2018 / Accepted: 21 May 2018 / Published: 15 June 2018
Cited by 2 | PDF Full-text (2982 KB) | HTML Full-text | XML Full-text
Abstract
The acid solubilised collagen (ASC) and pepsin solubilised collagen (PSC) were extracted from the by-products (skin) of a cartilaginous fish (Mustelus mustelus). The ASC and PSC yields were 23.07% and 35.27% dry weight, respectively and were identified as collagen Type I [...] Read more.
The acid solubilised collagen (ASC) and pepsin solubilised collagen (PSC) were extracted from the by-products (skin) of a cartilaginous fish (Mustelus mustelus). The ASC and PSC yields were 23.07% and 35.27% dry weight, respectively and were identified as collagen Type I with the presence of α, β and γ chains. As revealed by the Fourier Transform Infrared (FTIR) spectra analysis, pepsin did not alter the PSC triple helix structure. Based on the various type of collagen yield, only PSC was used in combination with chitosan to produce a composite film. Such film had lower tensile strength but higher elongation at break when compared to chitosan film; and lower water solubility and lightness when compared to collagen film. Equally, FTIR spectra analysis of film composite showed the occurrence of collagen-chitosan interaction resulting in a modification of the secondary structure of collagen. Collagen-chitosan-based biofilm showed a potential UV barrier properties and antioxidant activity, which might be used as green bioactive films to preserve nutraceutical products. Full article
(This article belongs to the Special Issue Collagen from Marine Biological Source and Medical Applications)
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Open AccessArticle
Production, Characterization and Biocompatibility Evaluation of Collagen Membranes Derived from Marine Sponge Chondrosia reniformis Nardo, 1847
Mar. Drugs 2018, 16(4), 111; https://doi.org/10.3390/md16040111
Received: 12 March 2018 / Revised: 22 March 2018 / Accepted: 27 March 2018 / Published: 29 March 2018
Cited by 3 | PDF Full-text (47826 KB) | HTML Full-text | XML Full-text
Abstract
Collagen is involved in the formation of complex fibrillar networks, providing the structural integrity of tissues. Its low immunogenicity and mechanical properties make this molecule a biomaterial that is extremely suitable for tissue engineering and regenerative medicine (TERM) strategies in human health issues. [...] Read more.
Collagen is involved in the formation of complex fibrillar networks, providing the structural integrity of tissues. Its low immunogenicity and mechanical properties make this molecule a biomaterial that is extremely suitable for tissue engineering and regenerative medicine (TERM) strategies in human health issues. Here, for the first time, we performed a thorough screening of four different methods to obtain sponge collagenous fibrillar suspensions (FSs) from C. reniformis demosponge, which were then chemically, physically, and biologically characterized, in terms of protein, collagen, and glycosaminoglycans content, viscous properties, biocompatibility, and antioxidant activity. These four FSs were then tested for their capability to generate crosslinked or not thin sponge collagenous membranes (SCMs) that are suitable for TERM purposes. Two types of FSs, of the four tested, were able to generate SCMs, either from crosslinking or not, and showed good mechanical properties, enzymatic degradation resistance, water binding capacity, antioxidant activity, and biocompatibility on both fibroblast and keratinocyte cell cultures. Finally, our results demonstrate that it is possible to adapt the extraction procedure in order to alternatively improve the mechanical properties or the antioxidant performances of the derived biomaterial, depending on the application requirements, thanks to the versatility of C. reniformis extracellular matrix extracts. Full article
(This article belongs to the Special Issue Collagen from Marine Biological Source and Medical Applications)
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Open AccessArticle
Unique Collagen Fibers for Biomedical Applications
Mar. Drugs 2018, 16(4), 102; https://doi.org/10.3390/md16040102
Received: 15 February 2018 / Revised: 9 March 2018 / Accepted: 17 March 2018 / Published: 23 March 2018
Cited by 4 | PDF Full-text (28404 KB) | HTML Full-text | XML Full-text
Abstract
The challenge to develop grafts for tissue regeneration lies in the need to obtain a scaffold that will promote cell growth in order to form new tissue at a trauma-damaged site. Scaffolds also need to provide compatible mechanical properties that will support the [...] Read more.
The challenge to develop grafts for tissue regeneration lies in the need to obtain a scaffold that will promote cell growth in order to form new tissue at a trauma-damaged site. Scaffolds also need to provide compatible mechanical properties that will support the new tissue and facilitate the desired physiological activity. Here, we used natural materials to develop a bio-composite made of unique collagen embedded in an alginate hydrogel material. The collagen fibers used to create the building blocks exhibited a unique hyper-elastic behavior similar to that of natural human tissue. The prominent mechanical properties, along with the support of cell adhesion affects cell shape and supports their proliferation, consequently facilitating the formation of a new tissue-like structure. The current study elaborates on these unique collagen fibers, focusing on their structure and biocompatibility, in an in vitro model. The findings suggest it as a highly appropriate material for biomedical applications. The promising in vitro results indicate that the distinctive collagen fibers could serve as a scaffold that can be adapted for tissue regeneration, in support of healing processes, along with maintaining tissue mechanical properties for the new regenerate tissue formation. Full article
(This article belongs to the Special Issue Collagen from Marine Biological Source and Medical Applications)
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Open AccessArticle
Biphasic Scaffolds from Marine Collagens for Regeneration of Osteochondral Defects
Mar. Drugs 2018, 16(3), 91; https://doi.org/10.3390/md16030091
Received: 10 January 2018 / Revised: 5 March 2018 / Accepted: 10 March 2018 / Published: 13 March 2018
Cited by 4 | PDF Full-text (12125 KB) | HTML Full-text | XML Full-text
Abstract
Background: Collagens of marine origin are applied increasingly as alternatives to mammalian collagens in tissue engineering. The aim of the present study was to develop a biphasic scaffold from exclusively marine collagens supporting both osteogenic and chondrogenic differentiation and to find a suitable [...] Read more.
Background: Collagens of marine origin are applied increasingly as alternatives to mammalian collagens in tissue engineering. The aim of the present study was to develop a biphasic scaffold from exclusively marine collagens supporting both osteogenic and chondrogenic differentiation and to find a suitable setup for in vitro chondrogenic and osteogenic differentiation of human mesenchymal stroma cells (hMSC). Methods: Biphasic scaffolds from biomimetically mineralized salmon collagen and fibrillized jellyfish collagen were fabricated by joint freeze-drying and crosslinking. Different experiments were performed to analyze the influence of cell density and TGF-β on osteogenic differentiation of the cells in the scaffolds. Gene expression analysis and analysis of cartilage extracellular matrix components were performed and activity of alkaline phosphatase was determined. Furthermore, histological sections of differentiated cells in the biphasic scaffolds were analyzed. Results: Stable biphasic scaffolds from two different marine collagens were prepared. An in vitro setup for osteochondral differentiation was developed involving (1) different seeding densities in the phases; (2) additional application of alginate hydrogel in the chondral part; (3) pre-differentiation and sequential seeding of the scaffolds and (4) osteochondral medium. Spatially separated osteogenic and chondrogenic differentiation of hMSC was achieved in this setup, while osteochondral medium in combination with the biphasic scaffolds alone was not sufficient to reach this ambition. Conclusions: Biphasic, but monolithic scaffolds from exclusively marine collagens are suitable for the development of osteochondral constructs. Full article
(This article belongs to the Special Issue Collagen from Marine Biological Source and Medical Applications)
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Open AccessArticle
Optimization of Extraction Conditions and Characterization of Pepsin-Solubilised Collagen from Skin of Giant Croaker (Nibea japonica)
Mar. Drugs 2018, 16(1), 29; https://doi.org/10.3390/md16010029
Received: 27 December 2017 / Revised: 6 January 2018 / Accepted: 10 January 2018 / Published: 14 January 2018
Cited by 5 | PDF Full-text (3943 KB) | HTML Full-text | XML Full-text
Abstract
In the present study, response surface methodology was performed to investigate the effects of extraction parameters on pepsin-solubilised collagen (PSC) from the skin of the giant croaker Nibea japonica. The optimum extraction conditions of PSC were as follows: concentration of pepsin was [...] Read more.
In the present study, response surface methodology was performed to investigate the effects of extraction parameters on pepsin-solubilised collagen (PSC) from the skin of the giant croaker Nibea japonica. The optimum extraction conditions of PSC were as follows: concentration of pepsin was 1389 U/g, solid-liquid ratio was 1:57 and hydrolysis time was 8.67 h. Under these conditions, the extraction yield of PSC was up to 84.85%, which is well agreement with the predict value of 85.03%. The PSC from Nibea japonica skin was then characterized as type I collagen by using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The fourier transforms infrared spetroscopy (FTIR) analysis revealed that PSC maintains its triple-helical structure by the hydrogen bond. All PSCs were soluble in the pH range of 1.0–4.0 and decreases in solubility were observed at neutral or alkaline conditions. All PSCs had a decrease in solubility in the presence of sodium chloride, especially with a concentration above 2%. So, the Nibea japonica skin could serve as another potential source of collagen. Full article
(This article belongs to the Special Issue Collagen from Marine Biological Source and Medical Applications)
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Open AccessArticle
Bioinspiring Chondrosia reniformis (Nardo, 1847) Collagen-Based Hydrogel: A New Extraction Method to Obtain a Sticky and Self-Healing Collagenous Material
Mar. Drugs 2017, 15(12), 380; https://doi.org/10.3390/md15120380
Received: 30 September 2017 / Revised: 28 October 2017 / Accepted: 16 November 2017 / Published: 4 December 2017
Cited by 2 | PDF Full-text (3728 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Collagen is a natural and abundant polymer that serves multiple functions in both invertebrates and vertebrates. As collagen is the natural scaffolding for cells, collagen-based hydrogels are regarded as ideal materials for tissue engineering applications since they can mimic the natural cellular microenvironment. [...] Read more.
Collagen is a natural and abundant polymer that serves multiple functions in both invertebrates and vertebrates. As collagen is the natural scaffolding for cells, collagen-based hydrogels are regarded as ideal materials for tissue engineering applications since they can mimic the natural cellular microenvironment. Chondrosia reniformis is a marine demosponge particularly rich in collagen, characterized by the presence of labile interfibrillar crosslinks similarly to those described in the mutable collagenous tissues (MCTs) of echinoderms. As a result single fibrils can be isolated using calcium-chelating and disulphide-reducing chemicals. In the present work we firstly describe a new extraction method that directly produces a highly hydrated hydrogel with interesting self-healing properties. The materials obtained were then biochemically and rheologically characterized. Our investigation has shown that the developed extraction procedure is able to extract collagen as well as other proteins and Glycosaminoglycans (GAG)-like molecules that give the collagenous hydrogel interesting and new rheological properties when compared to other described collagenous materials. The present work motivates further in-depth investigations towards the development of a new class of injectable collagenous hydrogels with tailored specifications. Full article
(This article belongs to the Special Issue Collagen from Marine Biological Source and Medical Applications)
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Open AccessArticle
Collagen from the Marine Sponges Axinella cannabina and Suberites carnosus: Isolation and Morphological, Biochemical, and Biophysical Characterization
Mar. Drugs 2017, 15(6), 152; https://doi.org/10.3390/md15060152
Received: 22 April 2017 / Revised: 22 April 2017 / Accepted: 25 May 2017 / Published: 29 May 2017
Cited by 13 | PDF Full-text (2337 KB) | HTML Full-text | XML Full-text
Abstract
In search of alternative and safer sources of collagen for biomedical applications, the marine demosponges Axinella cannabina and Suberites carnosus, collected from the Aegean and the Ionian Seas, respectively, were comparatively studied for their insoluble collagen, intercellular collagen, and spongin-like collagen content. [...] Read more.
In search of alternative and safer sources of collagen for biomedical applications, the marine demosponges Axinella cannabina and Suberites carnosus, collected from the Aegean and the Ionian Seas, respectively, were comparatively studied for their insoluble collagen, intercellular collagen, and spongin-like collagen content. The isolated collagenous materials were morphologically, physicochemically, and biophysically characterized. Using scanning electron microscopy and transmission electron microscopy the fibrous morphology of the isolated collagens was confirmed, whereas the amino acid analysis, in conjunction with infrared spectroscopy studies, verified the characteristic for the collagen amino acid profile and its secondary structure. Furthermore, the isoelectric point and thermal behavior were determined by titration and differential scanning calorimetry, in combination with circular dichroism spectroscopic studies, respectively. Full article
(This article belongs to the Special Issue Collagen from Marine Biological Source and Medical Applications)
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Review

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Open AccessReview
Collagen of Extracellular Matrix from Marine Invertebrates and Its Medical Applications
Mar. Drugs 2019, 17(2), 118; https://doi.org/10.3390/md17020118
Received: 22 December 2018 / Revised: 25 January 2019 / Accepted: 5 February 2019 / Published: 14 February 2019
Cited by 1 | PDF Full-text (5083 KB) | HTML Full-text | XML Full-text
Abstract
The extraction and purification of collagen are of great interest due to its biological function and medicinal applications. Although marine invertebrates are abundant in the animal kingdom, our knowledge of their extracellular matrix (ECM), which mainly contains collagen, is lacking. The functions of [...] Read more.
The extraction and purification of collagen are of great interest due to its biological function and medicinal applications. Although marine invertebrates are abundant in the animal kingdom, our knowledge of their extracellular matrix (ECM), which mainly contains collagen, is lacking. The functions of collagen isolated from marine invertebrates remain an untouched source of the proteinaceous component in the development of groundbreaking pharmaceuticals. This review will give an overview of currently used collagens and their future applications, as well as the methodological issues of collagens from marine invertebrates for potential drug discovery. Full article
(This article belongs to the Special Issue Collagen from Marine Biological Source and Medical Applications)
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Open AccessReview
Collagens of Poriferan Origin
Mar. Drugs 2018, 16(3), 79; https://doi.org/10.3390/md16030079
Received: 30 December 2017 / Revised: 3 February 2018 / Accepted: 28 February 2018 / Published: 3 March 2018
Cited by 8 | PDF Full-text (4914 KB) | HTML Full-text | XML Full-text
Abstract
The biosynthesis, structural diversity, and functionality of collagens of sponge origin are still paradigms and causes of scientific controversy. This review has the ambitious goal of providing thorough and comprehensive coverage of poriferan collagens as a multifaceted topic with intriguing hypotheses and numerous [...] Read more.
The biosynthesis, structural diversity, and functionality of collagens of sponge origin are still paradigms and causes of scientific controversy. This review has the ambitious goal of providing thorough and comprehensive coverage of poriferan collagens as a multifaceted topic with intriguing hypotheses and numerous challenging open questions. The structural diversity, chemistry, and biochemistry of collagens in sponges are analyzed and discussed here. Special attention is paid to spongins, collagen IV-related proteins, fibrillar collagens from demosponges, and collagens from glass sponge skeletal structures. The review also focuses on prospects and trends in applications of sponge collagens for technology, materials science and biomedicine. Full article
(This article belongs to the Special Issue Collagen from Marine Biological Source and Medical Applications)
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Open AccessReview
Facial Bone Reconstruction Using both Marine or Non-Marine Bone Substitutes: Evaluation of Current Outcomes in a Systematic Literature Review
Mar. Drugs 2018, 16(1), 27; https://doi.org/10.3390/md16010027
Received: 2 November 2017 / Revised: 12 December 2017 / Accepted: 22 December 2017 / Published: 13 January 2018
Cited by 21 | PDF Full-text (472 KB) | HTML Full-text | XML Full-text
Abstract
The aim of the present investigation was to systematically analyse the literature on the facial bone reconstruction defect using marine collagen or not and to evaluate a predictable treatment for their clinical management. The revision has been performed by searched MEDLINE and EMBASE [...] Read more.
The aim of the present investigation was to systematically analyse the literature on the facial bone reconstruction defect using marine collagen or not and to evaluate a predictable treatment for their clinical management. The revision has been performed by searched MEDLINE and EMBASE databases from 2007 to 2017. Clinical trials and animal in vitro studies that had reported the application of bone substitutes or not for bone reconstruction defect and using marine collagen or other bone substitute material were recorded following Preferred Reporting Items for Systematic Reviews and Meta-Analyses (PRISMA) guidelines. The first selection involved 1201 citations. After screening and evaluation of suitability, 39 articles were added at the revision process. Numerous discrepancies among the papers about bone defects morphology, surgical protocols, and selection of biomaterials were found. All selected manuscripts considered the final clinical success after the facial bone reconstruction applying bone substitutes. However, the scientific evidence regarding the vantage of the appliance of a biomaterial versus autologous bone still remains debated. Marine collagen seems to favor the dimensional stability of the graft and it could be an excellent carrier for growth factors. Full article
(This article belongs to the Special Issue Collagen from Marine Biological Source and Medical Applications)
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