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Marine Drugs
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Marine Collagen: A Promising Biomaterial for Biomedical Applications
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Marine Collagen: A Promising Biomaterial for Biomedical Applications

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

Deadline for manuscript submissions: closed (31 December 2020) | Viewed by 27731

Special Issue Editor

Dr. Sik Yoon

E-Mail Website
Guest Editor
Department of Anatomy, College of Medicine, Pusan National University, Yangsan 50612, Republic of Korea
Interests: biomaterials; 3D cell culture; organoids; marine biology; cancer; immunology; cell biology; thymus regeneration
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Marine Drugs invites submissions to this Special Issue on “Marine Collagen: A Promising Biomaterial for Biomedical Applications”. 

Collagen-based biomaterials are extensively applied in various biomedical fields, such as a scaffold in tissue engineering. However, there are many challenges facing the use of mammalian collagen, including the issues of religious constrains, an allergic or autoimmune reaction, and the spread of animal diseases such as bovine spongiform encephalopathy, transmissible spongiform encephalopathy, and foot-and-mouth disease. Over the past few decades, marine collagen (MC) has emerged as a promising biomaterial for biomedical applications due to its structural similarity to mammalian collagen. Marine organisms are a rich source of structurally novel and biologically active compounds, and to date, many biological components have been isolated from various marine resources. MC offers advantages over mammalian collagen due to its water solubility, easy extractability, low immunogenicity, safety, biocompatibility, biodegradability, antimicrobial activity, functionality, and low production costs. Due to its characteristics and physicobiochemical properties, it has tremendous potential for use as a scaffold biomaterial in tissue engineering and regenerative medicine, in drug delivery systems, and as a therapeutic.

In this Special Issue, we encourage submissions of the recent developments, advancements, trends, challenges, and future perspectives in this new research field. We expect to receive contributions from different areas of multidisciplinary research, including—but not restricted to—extraction, characterization, fabrication, and experimentation of MC, with a particular focus on their biomedical uses. Comprehensive review papers are also welcome in this Special Issue.

Dr. Sik Yoon
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 submissions that pass pre-check are 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 2900 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

  • Marine collagen
  • Biomaterials
  • Extraction, characterization, fabrication
  • 3D cell culture, bioprinting
  • Tissue engineering
  • Regenerative medicine
  • Drug delivery, therapy
  • Biomedical application

Related Special Issue

Published Papers (6 papers)

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Research

17 pages, 4015 KiB  
Article
Influences of Molecular Weights on Physicochemical and Biological Properties of Collagen-Alginate Scaffolds
by Truc Cong Ho, Jin-Seok Park, Sung-Yeoul Kim, Hoyeol Lee, Ju-Sop Lim, Shin-Jun Kim, Mi-Hee Choi, Seung Yun Nam and Byung-Soo Chun
Mar. Drugs 2021, 19(2), 85; https://doi.org/10.3390/md19020085 - 02 Feb 2021
Cited by 7 | Viewed by 2169
Abstract
For tissue engineering applications, biodegradable scaffolds containing high molecular weights (MW) of collagen and sodium alginate have been developed and characterized. However, the properties of low MW collagen-based scaffolds have not been studied in previous research. This work examined the distinctive properties of [...] Read more.
For tissue engineering applications, biodegradable scaffolds containing high molecular weights (MW) of collagen and sodium alginate have been developed and characterized. However, the properties of low MW collagen-based scaffolds have not been studied in previous research. This work examined the distinctive properties of low MW collagen-based scaffolds with alginate unmodified and modified by subcritical water. Besides, we developed a facile method to cross-link water-soluble scaffolds using glutaraldehyde in an aqueous ethanol solution. The prepared cross-linked scaffolds showed good structural properties with high porosity (~93%) and high cross-linking degree (50–60%). Compared with collagen (6000 Da)-based scaffolds, collagen (25,000 Da)-based scaffolds exhibited higher stability against collagenase degradation and lower weight loss in phosphate buffer pH 7.4. Collagen (25,000 Da)-based scaffolds with modified alginate tended to improve antioxidant capacity compared with scaffolds containing unmodified alginate. Interestingly, in vitro coagulant activity assay demonstrated that collagen (25,000 Da)-based scaffolds with modified alginate (C25-A63 and C25-A21) significantly reduced the clotting time of human plasma compared with scaffolds consisting of unmodified alginate. Although some further investigations need to be done, collagen (25,000 Da)-based scaffolds with modified alginate should be considered as a potential candidate for tissue engineering applications. Full article
(This article belongs to the Special Issue Marine Collagen: A Promising Biomaterial for Biomedical Applications)
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18 pages, 1714 KiB  
Article
Extraction and Characterization of Collagen from Elasmobranch Byproducts for Potential Biomaterial Use
by Manuel J. Seixas, Eva Martins, Rui L. Reis and Tiago H. Silva
Mar. Drugs 2020, 18(12), 617; https://doi.org/10.3390/md18120617 - 04 Dec 2020
Cited by 32 | Viewed by 4902
Abstract
With the worldwide increase of fisheries, fish wastes have had a similar increase, alternatively they can be seen as a source of novel substances for the improvement of society’s wellbeing. Elasmobranchs are a subclass fished in high amounts, with some species being mainly [...] Read more.
With the worldwide increase of fisheries, fish wastes have had a similar increase, alternatively they can be seen as a source of novel substances for the improvement of society’s wellbeing. Elasmobranchs are a subclass fished in high amounts, with some species being mainly bycatch. They possess an endoskeleton composed mainly by cartilage, from which chondroitin sulfate is currently obtained. Their use as a viable source for extraction of type II collagen has been hypothesized with the envisaging of a biomedical application, namely in biomaterials production. In the present work, raw cartilage from shark (Prionace glauca) and ray (Zeachara chilensis and Bathyraja brachyurops) was obtained from a fish processing company and submitted to acidic and enzymatic extractions, to produce acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC). From all the extractions, P. glauca PSC had the highest yield (3.5%), followed by ray ASC (0.92%), ray PSC (0.50%), and P. glauca ASC (0.15%). All the extracts showed similar properties, with the SDS-PAGE profiles being compatible with the presence of both type I and type II collagens. Moreover, the collagen extracts exhibited the competence to maintain their conformation at human basal temperature, presenting a denaturation temperature higher than 37 °C. Hydrogels were produced using P. glauca PSC combined with shark chondroitin sulfate, with the objective of mimicking the human cartilage extracellular matrix. These hydrogels were cohesive and structurally-stable at 37 °C, with rheological measurements exhibiting a conformation of an elastic solid when submitted to shear strain with a frequency up to 4 Hz. This work revealed a sustainable strategy for the valorization of fisheries’ by-products, within the concept of a circular economy, consisting of the use of P. glauca, Z. chilensis, and B. brachyurops cartilage for the extraction of collagen, which would be further employed in the development of hydrogels as a proof of concept of its biotechnological potential, ultimately envisaging its use in marine biomaterials to regenerate damaged cartilaginous tissues. Full article
(This article belongs to the Special Issue Marine Collagen: A Promising Biomaterial for Biomedical Applications)
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27 pages, 17156 KiB  
Article
A Marine Collagen-Based Biomimetic Hydrogel Recapitulates Cancer Stem Cell Niche and Enhances Progression and Chemoresistance in Human Ovarian Cancer
by SooHyeon Moon, YeJin Ok, SeonYeong Hwang, Ye Seon Lim, Hye-Yoon Kim, Yong-Jin Na and Sik Yoon
Mar. Drugs 2020, 18(10), 498; https://doi.org/10.3390/md18100498 - 29 Sep 2020
Cited by 8 | Viewed by 3249
Abstract
Recent attention has focused on the development of an effective three-dimensional (3D) cell culture system enabling the rapid enrichment of cancer stem cells (CSCs) that are resistant to therapies and serving as a useful in vitro tumor model that accurately reflects in vivo [...] Read more.
Recent attention has focused on the development of an effective three-dimensional (3D) cell culture system enabling the rapid enrichment of cancer stem cells (CSCs) that are resistant to therapies and serving as a useful in vitro tumor model that accurately reflects in vivo behaviors of cancer cells. Presently, an effective 3D in vitro model of ovarian cancer (OC) was developed using a marine collagen-based hydrogel. Advantages of the model include simplicity, efficiency, bioactivity, and low cost. Remarkably, OC cells grown in this hydrogel exhibited biochemical and physiological features, including (1) enhanced cell proliferation, migration and invasion, colony formation, and chemoresistance; (2) suppressed apoptosis with altered expression levels of apoptosis-regulating molecules; (3) upregulated expression of crucial multidrug resistance-related genes; (4) accentuated expression of key molecules associated with malignant progression, such as epithelial–mesenchymal transition transcription factors, Notch, and pluripotency biomarkers; and (5) robust enrichment of ovarian CSCs. The findings indicate the potential of our 3D in vitro OC model as an in vitro research platform to study OC and ovarian CSC biology and to screen novel therapies targeting OC and ovarian CSCs. Full article
(This article belongs to the Special Issue Marine Collagen: A Promising Biomaterial for Biomedical Applications)
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14 pages, 2095 KiB  
Article
Physicochemical Properties of Collagen from Acaudina Molpadioides and Its Protective Effects against H2O2-Induced Injury in RAW264.7 Cells
by Jie Li, Yan Li, Yuyao Li, Zuisu Yang and Huoxi Jin
Mar. Drugs 2020, 18(7), 370; https://doi.org/10.3390/md18070370 - 18 Jul 2020
Cited by 20 | Viewed by 3326
Abstract
Collagen is a promising biomaterial used in the beauty and biomedical industries. In this study, the physicochemical characterization, antioxidant activities, and protective effects against H2O2-induced injury of collagen isolated from Acaudina molpadioides were investigated. The amino acid composition analysis [...] Read more.
Collagen is a promising biomaterial used in the beauty and biomedical industries. In this study, the physicochemical characterization, antioxidant activities, and protective effects against H2O2-induced injury of collagen isolated from Acaudina molpadioides were investigated. The amino acid composition analysis showed that the collagen was rich in glycine (Gly), alanine (Ala), and glutamic acid (Glu), but poor in tyrosine (Tyr) and phenylalanine (Phe). Zeta potential analysis revealed that the isoelectric point (pI) of collagen from Acaudina molpadioides was about 4.25. It possessed moderate scavenging activities of 2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,2’-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid (ABTS) radicals in a dose-dependent manner. In addition, the collagen was able to effectively improve cell viability and morphology, inhibit the production of Malondialdehyde (MDA), and increase the activities of Superoxide Dismutase (SOD) and Glutathione Peroxidase (GSH-Px) in cultured RAW264.7 cells, resulting in a protective effect against H2O2-induced injury. Overall, the results showed that collagen extracted from A. molpadioides has promising prospects in the beauty and cosmetics industries. Full article
(This article belongs to the Special Issue Marine Collagen: A Promising Biomaterial for Biomedical Applications)
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9 pages, 2619 KiB  
Article
Enzymatic Hydrolysis of Marine Collagen and Fibrinogen Proteins in the Presence of Thrombin
by Ludmila L. Semenycheva, Marfa N. Egorikhina, Victoria O. Chasova, Natalya B. Valetova, Yulia L. Kuznetsova and Alexander V. Mitin
Mar. Drugs 2020, 18(4), 208; https://doi.org/10.3390/md18040208 - 11 Apr 2020
Cited by 9 | Viewed by 2949
Abstract
Enzymatic hydrolysis of native collagen and fibrinogen was carried out under comparable conditions at room temperature. The molecular weight parameters of proteins before and after hydrolysis by thrombin were monitored by gel-penetrating chromatography (GPC). An analysis of the experiment results shows that the [...] Read more.
Enzymatic hydrolysis of native collagen and fibrinogen was carried out under comparable conditions at room temperature. The molecular weight parameters of proteins before and after hydrolysis by thrombin were monitored by gel-penetrating chromatography (GPC). An analysis of the experiment results shows that the molecular weight parameters of the initial fibrinogen (Fn) and cod collagen (CC) are very similar. High molecular CC decays within the first minute, forming two low molecular fractions. The main part (~80%) falls on the fraction with a value of Mw less than 10 kDa. The initial high molecular fraction of Fn with Mw ~320–340 kDa is not completely hydrolyzed even after three days of control. The presence of low molecular fractions with Mw ~17 and Mw ~10 kDa in the solution slightly increases within an hour and noticeably increases for three days. The destruction of macromolecules of high molecular collagen to hydrolysis products appears almost completely within the first minute mainly to the polymer with Mw ~10 kDa, and enzymatic hydrolysis of fibrinogen proceeds slower than that of collagen, but also mainly to the polymer with Mw ~10 kDa. Comparative photos of the surfaces of native collagen, fibrinogen and the scaffold based on them were obtained. Full article
(This article belongs to the Special Issue Marine Collagen: A Promising Biomaterial for Biomedical Applications)
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16 pages, 5862 KiB  
Article
Comprehensive Assessment of Nile Tilapia Skin (Oreochromis niloticus) Collagen Hydrogels for Wound Dressings
by Baosheng Ge, Haonan Wang, Jie Li, Hengheng Liu, Yonghao Yin, Naili Zhang and Song Qin
Mar. Drugs 2020, 18(4), 178; https://doi.org/10.3390/md18040178 - 25 Mar 2020
Cited by 80 | Viewed by 10436
Abstract
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue Marine Collagen: A Promising Biomaterial for Biomedical Applications)
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