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Marine Drugs
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Fundamentals and Biomedical Applications of Marine Collagen
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Fundamentals and Biomedical Applications of Marine Collagen

A special issue of Marine Drugs (ISSN 1660-3397). This special issue belongs to the section "Biomaterials of Marine Origin".

Deadline for manuscript submissions: 31 May 2024 | Viewed by 8647

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,

Recently, there has been rapidly growing interest in biomaterials for a variety of in vitro and in vivo biomedical research and applications. Particularly, collagen-based biomaterials have been extensively applied in various biomedical fields, such as scaffolds in tissue engineering. However, there are many challenges associated with the use of mammalian collagen, including the issues of religious constraints, allergic or autoimmune reactions, and the spread of animal diseases. Over the past few decades, marine collagen (MC) has emerged as a promising biomaterial for pharmacological and biomedical applications. Marine organisms are a rich source of collagen, and 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 related to 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, from fundamentals (including extraction, purification, characterization, fabrication, and experimentation) to biotechnological, pharmacological, biomedical, and therapeutic applications of MC. 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
  • extraction, purification, characterization, synthesis
  • scaffold, 3D cell culture, spheroid, tumoroid, organoid
  • biomaterial, biofabrication, nanofiber, nanocarrier
  • polymer, hydrogel, bioink, bioprinting
  • cytoprotection, tissue repair, regenerative medicine
  • tissue engineering, biomedical engineering, artificial organ
  • drug delivery, nanomedicine
  • disease modeling, diagnostic or therapeutic application
  • biomedical, pharmacological or biotechnological application

Related Special Issue

Published Papers (6 papers)

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Research

12 pages, 6492 KiB  
Article
The Influence of Various Crosslinking Conditions of EDC/NHS on the Properties of Fish Collagen Film
by Alina Sionkowska, Karolina Kulka-Kamińska, Patrycja Brudzyńska, Katarzyna Lewandowska and Łukasz Piwowarski
Mar. Drugs 2024, 22(5), 194; https://doi.org/10.3390/md22050194 - 25 Apr 2024
Abstract
The process of crosslinking improves the physicochemical properties of biopolymer-based composites, making them valuable for biomedical applications. EDC/NHS-crosslinked collagen materials have a significant potential for tissue engineering applications, due to their enhanced properties and biocompatibility. Chemical crosslinking of samples can be carried out [...] Read more.
The process of crosslinking improves the physicochemical properties of biopolymer-based composites, making them valuable for biomedical applications. EDC/NHS-crosslinked collagen materials have a significant potential for tissue engineering applications, due to their enhanced properties and biocompatibility. Chemical crosslinking of samples can be carried out in several ways, which is crucial and has a direct effect on the final properties of the obtained material. In this study, the effect of crosslinking conditions on the properties of collagen films using EDC and NHS was investigated. Studies included FTIR spectroscopy, AFM, swelling and degradation tests, mechanical testing and contact angle measurements. Evaluation of prepared collagen films indicated that both crosslinking agents and crosslinking conditions influenced film properties. Notable alternations were observed in the infrared spectrum of the sample, to which EDC was added directly to the fish collagen solution. The same sample indicated the lowest Young modulus, tensile strength and breaking force parameters and the highest elongation at break. All samples reached the maximum swelling degree two hours after immersion in PBS solution; however, the immersion-crosslinked samples exhibited a significantly lower degree of swelling and were highly durable. The highest roughness was observed for the collagen film crosslinked with EDC, whereas the lowest was observed for the specimen crosslinked with EDC with NHS addition. The crosslinking agents increased the surface roughness of the collagen film, except for the sample modified with the addition of EDC and NHS mixture. All films were characterized by hydrophilic character. The films’ modification resulted in a decrease in their hydrophilicity and wettability. Our research allows for a comparison of proposed EDC/NHS crosslinking conditions and their influence on the physicochemical properties of fish collagen thin films. EDC and NHS are promising crosslinking agents for the modification of fish collagen used in biomedical applications. Full article
(This article belongs to the Special Issue Fundamentals and Biomedical Applications of Marine Collagen)
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33 pages, 5676 KiB  
Article
Fish Collagen Peptides Enhance Thymopoietic Gene Expression, Cell Proliferation, Thymocyte Adherence, and Cytoprotection in Thymic Epithelial Cells via Activation of the Nuclear Factor-κB Pathway, Leading to Thymus Regeneration after Cyclophosphamide-Induced Injury
by Do Young Lee, Won Hoon Song, Ye Seon Lim, Changyong Lee, Lata Rajbongshi, Seon Yeong Hwang, Byoung Soo Kim, Dongjun Lee, Yong Jung Song, Hwi-Gon Kim and Sik Yoon
Mar. Drugs 2023, 21(10), 531; https://doi.org/10.3390/md21100531 - 12 Oct 2023
Viewed by 1563
Abstract
Prolonged thymic involution results in decreased thymopoiesis and thymic output, leading to peripheral T-cell deficiency. Since the thymic-dependent pathway is the only means of generating fully mature T cells, the identification of strategies to enhance thymic regeneration is crucial in developing therapeutic interventions [...] Read more.
Prolonged thymic involution results in decreased thymopoiesis and thymic output, leading to peripheral T-cell deficiency. Since the thymic-dependent pathway is the only means of generating fully mature T cells, the identification of strategies to enhance thymic regeneration is crucial in developing therapeutic interventions to revert immune suppression in immunocompromised patients. The present study clearly shows that fish collagen peptides (FCPs) stimulate activities of thymic epithelial cells (TECs), including cell proliferation, thymocyte adhesion, and the gene expression of thymopoietic factors such as FGF-7, IGF-1, BMP-4, VEGF-A, IL-7, IL-21, RANKL, LTβ, IL-22R, RANK, LTβR, SDF-1, CCL21, CCL25, CXCL5, Dll1, Dll4, Wnt4, CD40, CD80, CD86, ICAM-1, VCAM-1, FoxN1, leptin, cathepsin L, CK5, and CK8 through the NF-κB signal transduction pathway. Furthermore, our study also revealed the cytoprotective effects of FCPs on TECs against cyclophosphamide-induced cellular injury through the NF-κB signaling pathway. Importantly, FCPs exhibited a significant capability to facilitate thymic regeneration in mice after cyclophosphamide-induced damage via the NF-κB pathway. Taken together, this study sheds light on the role of FCPs in TEC function, thymopoiesis, and thymic regeneration, providing greater insight into the development of novel therapeutic strategies for effective thymus repopulation for numerous clinical conditions in which immune reconstitution is required. Full article
(This article belongs to the Special Issue Fundamentals and Biomedical Applications of Marine Collagen)
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14 pages, 5916 KiB  
Article
Influences of Trypsin Pretreatment on the Structures, Composition, and Functional Characteristics of Skin Gelatin of Tilapia, Grass Carp, and Sea Perch
by Qiufeng Ruan, Weijie Chen, Min Lv, Rong Zhang, Xu Luo, Ermeng Yu, Chuanyan Pan and Huawei Ma
Mar. Drugs 2023, 21(8), 423; https://doi.org/10.3390/md21080423 - 25 Jul 2023
Viewed by 1079
Abstract
Fish skin gelatin is an important functional product in the food, cosmetics, and biomedicine industries, and establishing a green and effective fish skin gelatin extraction method is an effective way to obtain high-quality gelatin and improve its production efficiency. In this study, a [...] Read more.
Fish skin gelatin is an important functional product in the food, cosmetics, and biomedicine industries, and establishing a green and effective fish skin gelatin extraction method is an effective way to obtain high-quality gelatin and improve its production efficiency. In this study, a trypsin method was used to extract the skin gelatin of sea perch, tilapia, and grass carp, and the microstructures of skin gelatin of these three fish species were analyzed, with such functional characteristics as thermal stability, gel strength, and emulsifying properties measured. The study results show that the skin gelatin of sea perch and tilapia obtained through the trypsin method has a relatively big molecular mass, a dense network structure, and a stable trihelix conformation. In addition, the skin gelatin of these three fish species has a relatively high β-turn content in the secondary structure, good gel strength, and water absorption properties. The compositions of the collagen-associated proteins in the skin gelatins of these three fish species extracted with the trypsin method are significantly different from each other, with positive effects of decorin and biglycan on the stability of the network structure of gelatin and a certain damaging effect of metalloendopeptidase on the network structure of gelatin. The skin gelatin of tilapia has high thermal stability and good emulsifying performance. Therefore, this gelatin type has bright application prospects in such fields as food processing, cosmetics, and drug development. In contrast, the skin gelatin of grass carp has poor functional properties. Therefore, there are significant differences among the structures and functions of skin gelatin extracted from different kinds of fish through the trypsin method. This finding has provided a useful reference for the production of customized fish gelatin according to demand. Full article
(This article belongs to the Special Issue Fundamentals and Biomedical Applications of Marine Collagen)
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13 pages, 3184 KiB  
Article
In Vitro Biodegradation, Drug Absorption, and Physical Properties of Gelatin–Fucoidan Microspheres Made of Subcritical-Water-Modified Fish Gelatin
by Truc Cong Ho, Ju-Sop Lim, Shin-Jun Kim, Sung-Yeoul Kim and Byung-Soo Chun
Mar. Drugs 2023, 21(5), 287; https://doi.org/10.3390/md21050287 - 03 May 2023
Cited by 3 | Viewed by 1269
Abstract
This study aimed to prepare gelatin–fucoidan microspheres with enhanced doxorubicin binding efficiency and controllable biodegradation using fish gelatin combined with low molecular weight (LMW) gelatin and fucoidan at fixed ratios. The MW of gelatin was modified by subcritical water (SW), which is known [...] Read more.
This study aimed to prepare gelatin–fucoidan microspheres with enhanced doxorubicin binding efficiency and controllable biodegradation using fish gelatin combined with low molecular weight (LMW) gelatin and fucoidan at fixed ratios. The MW of gelatin was modified by subcritical water (SW), which is known as a safe solvent, at 120 °C, 140 °C, and 160 °C. In addition, gelatin–fucoidan microspheres were prepared using a solvent exchange technique. Our findings revealed that particle size decreased, the surface was rougher, the swelling ratio increased, and particle shape was irregular in microspheres composed of SW-modified gelatin. Doxorubicin binding efficiency was improved by fucoidan and SW-modified gelatin at 120 °C but not at 140 °C and 160 °C. Interestingly, an increase in in vitro enzymatic degradation was observed in the microspheres consisting of SW-modified fish gelatin, although the cross-linking degree between them was not significantly different. This is because LMW gelatin could form more cross-linked bonds, which might be weaker than the intramolecular bonds of gelatin molecules. Gelatin–fucoidan microspheres consisting of SW-modified fish gelatin with controlled biodegradation rates could be a candidate for a short-term transient embolization agent. In addition, SW would be a promising method to modify the MW of gelatin for medical applications. Full article
(This article belongs to the Special Issue Fundamentals and Biomedical Applications of Marine Collagen)
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16 pages, 12119 KiB  
Article
Isolation and Biochemical Properties of Type II Collagen from Blue Shark (Prionace glauca) Cartilage
by Zhilin Pan, Baolin Ge, Mingjun Wei, Jeevithan Elango and Wenhui Wu
Mar. Drugs 2023, 21(5), 260; https://doi.org/10.3390/md21050260 - 23 Apr 2023
Cited by 5 | Viewed by 2259
Abstract
Numerous studies have shown that type II collagen (CII) has a potential role in the treatment of rheumatoid arthritis. However, most of the current studies have used terrestrial animal cartilage as a source of CII extraction, with fewer studies involving marine organisms. Based [...] Read more.
Numerous studies have shown that type II collagen (CII) has a potential role in the treatment of rheumatoid arthritis. However, most of the current studies have used terrestrial animal cartilage as a source of CII extraction, with fewer studies involving marine organisms. Based on this background, collagen (BSCII) was isolated from blue shark (Prionace glauca) cartilage by pepsin hydrolysis and its biochemical properties including protein pattern, total sugar content, microstructure, amino acid composition, spectral characteristics and thermal stability were further investigated in the present study. The SDS-PAGE results confirmed the typical characteristic of CII, comprising three identical α1 chains and its dimeric β chain. BSCII had the fibrous microstructure typical of collagen and an amino acid composition represented by high glycine content. BSCII had the typical UV and FTIR spectral characteristics of collagen. Further analysis revealed that BSCII had a high purity, while its secondary structure comprised 26.98% of β-sheet, 35.60% of β-turn, 37.41% of the random coil and no α-helix. CD spectra showed the triple helical structure of BSCII. The total sugar content, denaturation temperature and melting temperature of BSCII were (4.20 ± 0.03)%, 42 °C and 49 °C, respectively. SEM and AFM images confirmed a fibrillar and porous structure of collagen and denser fibrous bundles formed at higher concentrations. Overall, CII was successfully extracted from blue shark cartilage in the present study, and its molecular structure was intact. Therefore, blue shark cartilage could serve as a potential source for CII extraction with applications in biomedicine. Full article
(This article belongs to the Special Issue Fundamentals and Biomedical Applications of Marine Collagen)
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15 pages, 5170 KiB  
Article
Extraction and Characterization of Pepsin- and Acid-Soluble Collagen from the Swim Bladders of Megalonibea fusca
by Chou Mo, Qiaoli Wang, Guangfeng Li, Wanwen Dong, Feng Liang, Chaoxi Wu, Zhiping Wang and Yifei Wang
Mar. Drugs 2023, 21(3), 159; https://doi.org/10.3390/md21030159 - 27 Feb 2023
Cited by 7 | Viewed by 1790
Abstract
There is a growing demand for the identification of alternative sources of collagen not derived from land-dwelling animals. The present study explored the use of pepsin- and acid-based extraction protocols to isolate collagen from the swim bladders of Megalonibea fusca. After extraction, [...] Read more.
There is a growing demand for the identification of alternative sources of collagen not derived from land-dwelling animals. The present study explored the use of pepsin- and acid-based extraction protocols to isolate collagen from the swim bladders of Megalonibea fusca. After extraction, these acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) samples respectively were subjected to spectral analyses and sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) characterization, revealing both to be comprised of type I collagen with a triple-helical structure. The imino acid content of these ASC and PSC samples was 195 and 199 residues per 1000 residues, respectively. Scanning electron microscopy demonstrated that samples of freeze-dried collagen exhibited a compact lamellar structure, while transmission electron microscopy and atomic force microscopy confirmed the ability of these collagens to undergo self-assembly into fibers. ASC samples exhibited a larger fiber diameter than the PSC samples. The solubility of both ASC and PSC was highest under acidic pH conditions. Neither ASC nor PSC caused any cytotoxicity when tested in vitro, which met one of the requirements for the biological evaluation of medical devices. Thus, collagen isolated from the swim bladders of Megalonibea fusca holds great promise as a potential alternative to mammalian collagen. Full article
(This article belongs to the Special Issue Fundamentals and Biomedical Applications of Marine Collagen)
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