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Biomedical and Pharmacological Applications of Marine Collagen

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

Deadline for manuscript submissions: closed (30 November 2022) | Viewed by 25214

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Special Issue Editor

Dr. Sik Yoon

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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 “Biomedical and Pharmacological Applications of Marine Collagen”.

Biomimetic polymers and materials have been widely used in a variety of biomedical and pharmacological 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 constrains, allergic or autoimmune reactions, 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 and pharmacological applications. 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 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, including—but not restricted to—extraction, purification, characterization, fabrication, and experimentation of MC, with a particular focus on their biotechnological, biomedical and pharmacological 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
Extraction, purification, characterization, synthesis and fabrication
Biological activity
3D cell culture, bioprinting and organoids
Tissue engineering and regenerative medicine
Nanomedicine and drug delivery
Therapy and theranostics
Biomedical, pharmacological, nutraceutical and biotechnological applications

Related Special Issues

Marine Collagen: A Promising Biomaterial for Biomedical Applications in Marine Drugs (6 articles)
Fundamentals and Biomedical Applications of Marine Collagen in Marine Drugs (6 articles)

Published Papers (10 papers)

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Research

24 pages, 6045 KiB

Open AccessArticle

3D Biocomposites Comprising Marine Collagen and Silica-Based Materials Inspired on the Composition of Marine Sponge Skeletons Envisaging Bone Tissue Regeneration

by Eva Martins, Gabriela S. Diogo, Ricardo Pires, Rui L. Reis and Tiago H. Silva

Mar. Drugs 2022, 20(11), 718; https://0-doi-org.brum.beds.ac.uk/10.3390/md20110718 - 16 Nov 2022

Cited by 10 | Viewed by 2281

Abstract

Ocean resources are a priceless repository of unique species and bioactive compounds with denouement properties that can be used in the fabrication of advanced biomaterials as new templates for supporting the cell culture envisaging tissue engineering approaches. The collagen of marine origin can be sustainably isolated from the underrated fish processing industry by-products, while silica and related materials can be found in the spicules of marine sponges and diatoms frustules. Aiming to address the potential of biomaterials composed from marine collagen and silica-based materials in the context of bone regeneration, four different 3D porous structure formulations (COL, COL:BG, COL:D.E, and COL:BS) were fabricated by freeze-drying. The skins of Atlantic cod (Gadus morhua) were used as raw materials for the collagen (COL) isolation, which was successfully characterized by SDS-PAGE, FTIR, CD, and amino acid analyses, and identified as a type I collagen, produced with a 1.5% yield and a preserved characteristic triple helix conformation. Bioactive glass 45S5 bioglass^® (BG), diatomaceous earth (D.E.) powder, and biosilica (BS) isolated from the Axinella infundibuliformis sponge were chosen as silica-based materials, which were obtained as microparticles and characterized by distinct morphological features. The biomaterials revealed microporous structures, showing a porosity higher than 85%, a mean pore size range of 138–315 μm depending on their composition, with 70% interconnectivity which can be favorable for cell migration and ensure the needed nutrient supply. In vitro, biological assays were conducted by culturing L929 fibroblast-like cells, which confirmed not only the non-toxic nature of the developed biomaterials but also their capability to support cell adhesion and proliferation, particularly the COL:BS biomaterials, as observed by calcein-AM staining upon seven days of culture. Moreover, phalloidin and DAPI staining revealed well-spread cells, populating the entire construct. This study established marine collagen/silica biocomposites as potential scaffolds for tissue engineering, setting the basis for future studies, particularly envisaging the regeneration of non-load-bearing bone tissues. Full article

(This article belongs to the Special Issue Biomedical and Pharmacological Applications of Marine Collagen)

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15 pages, 7383 KiB

Open AccessArticle

Growth Factor-Free Vascularization of Marine-Origin Collagen Sponges Using Cryopreserved Stromal Vascular Fractions from Human Adipose Tissue

by Sara Freitas-Ribeiro, Gabriela S. Diogo, Catarina Oliveira, Albino Martins, Tiago H. Silva, Mariana Jarnalo, Ricardo Horta, Rui L. Reis and Rogério P. Pirraco

Mar. Drugs 2022, 20(10), 623; https://0-doi-org.brum.beds.ac.uk/10.3390/md20100623 - 30 Sep 2022

Cited by 2 | Viewed by 1850

Abstract

The successful integration of transplanted three-dimensional tissue engineering (TE) constructs depends greatly on their rapid vascularization. Therefore, it is essential to address this vascularization issue in the initial design of constructs for perfused tissues. Two of the most important variables in this regard are scaffold composition and cell sourcing. Collagens with marine origins overcome some issues associated with mammal-derived collagen while maintaining their advantages in terms of biocompatibility. Concurrently, the freshly isolated stromal vascular fraction (SVF) of adipose tissue has been proposed as an advantageous cell fraction for vascularization purposes due to its highly angiogenic properties, allowing extrinsic angiogenic growth factor-free vascularization strategies for TE applications. In this study, we aimed at understanding whether marine collagen 3D matrices could support cryopreserved human SVF in maintaining intrinsic angiogenic properties observed for fresh SVF. For this, cryopreserved human SVF was seeded on blue shark collagen sponges and cultured up to 7 days in a basal medium. The secretome profile of several angiogenesis-related factors was studied throughout culture times and correlated with the expression pattern of CD31 and CD146, which showed the formation of a prevascular network. Upon in ovo implantation, increased vessel recruitment was observed in prevascularized sponges when compared with sponges without SVF cells. Immunohistochemistry for CD31 demonstrated the improved integration of prevascularized sponges within chick chorioalantoic membrane (CAM) tissues, while in situ hybridization showed human cells lining blood vessels. These results demonstrate the potential of using cryopreserved SVF combined with marine collagen as a streamlined approach to improve the vascularization of TE constructs. Full article

(This article belongs to the Special Issue Biomedical and Pharmacological Applications of Marine Collagen)

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20 pages, 8475 KiB

Open AccessArticle

Preparation and Characterization of Tilapia Collagen-Thermoplastic Polyurethane Composite Nanofiber Membranes

by Sijia Wu, Longhe Yang and Junde Chen

Mar. Drugs 2022, 20(7), 437; https://0-doi-org.brum.beds.ac.uk/10.3390/md20070437 - 30 Jun 2022

Cited by 2 | Viewed by 1825

Abstract

Marine collagen is an ideal material for tissue engineering due to its excellent biological properties. However, the limited mechanical properties and poor stability of marine collagen limit its application in tissue engineering. Here, collagen was extracted from the skin of tilapia (Oreochromis nilotica). Collagen-thermoplastic polyurethane (Col-TPU) fibrous membranes were prepared using tilapia collagen as a foundational material, and their physicochemical and biocompatibility were investigated. Fourier transform infrared spectroscopy results showed that thermoplastic polyurethane was successfully combined with collagen, and the triple helix structure of collagen was retained. X-ray diffraction and differential scanning calorimetry results showed relatively good compatibility between collagen and TPU.SEM results showed that the average diameter of the composite nanofiber membrane decreased with increasing thermoplastic polyurethane proportion. The mechanical evaluation and thermogravimetric analysis showed that the thermal stability and tensile properties of Col-TPU fibrous membranes were significantly improved with increasing TPU. Cytotoxicity experiments confirmed that fibrous membranes with different ratios of thermoplastic polyurethane content showed no significant toxicity to fibroblasts; Col-TPU fibrous membranes were conducive to the migration and adhesion of cells. Thus, these Col-TPU composite nanofiber membranes might be used as a potential biomaterial in tissue regeneration. Full article

(This article belongs to the Special Issue Biomedical and Pharmacological Applications of Marine Collagen)

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14 pages, 6691 KiB

Open AccessArticle

Comparison of Physicochemical and Structural Properties of Acid-Soluble and Pepsin-Soluble Collagens from Blacktip Reef Shark Skin

by Baolin Ge, Chunyu Hou, Bin Bao, Zhilin Pan, José Eduardo Maté Sánchez de Val, Jeevithan Elango and Wenhui Wu

Mar. Drugs 2022, 20(6), 376; https://0-doi-org.brum.beds.ac.uk/10.3390/md20060376 - 02 Jun 2022

Cited by 6 | Viewed by 2447

Abstract

Fish collagen has been widely used in tissue engineering (TE) applications as an implant, which is generally transplanted into target tissue with stem cells for better regeneration ability. In this case, the success rate of this research depends on the fundamental components of fish collagen such as amino acid composition, structural and rheological properties. Therefore, researchers have been trying to find an innovative raw material from marine origins for tissue engineering applications. Based on this concept, collagens such as acid-soluble (ASC) and pepsin-soluble (PSC) were extracted from a new type of cartilaginous fish, the blacktip reef shark, for the first time, and were further investigated for physicochemical, protein pattern, microstructural and peptide mapping. The study results confirmed that the extracted collagens resemble the protein pattern of type-I collagen comprising the α₁, α₂, β and γ chains. The hydrophobic amino acids were dominant in both collagens with glycine and hydroxyproline as major amino acids. From the FTIR spectra, α helix (27.72 and 26.32%), β-sheet (22.24 and 23.35%), β-turn (21.34 and 22.08%), triple helix (14.11 and 14.13%) and random coil (14.59 and 14.12%) structures of ASC and PSC were confirmed, respectively. Collagens retained their triple helical and secondary structure well. Both collagens had maximum solubility at 3% NaCl and pH 4, and had absorbance maxima at 234 nm, respectively. The peptide mapping was almost similar for ASC and PSC at pH 2, generating peptides ranging from 15 to 200 kDa, with 23 kDa as a major peptide fragment. The microstructural analysis confirmed the homogenous fibrillar nature of collagens with more interconnected networks. Overall, the preset study concluded that collagen can be extracted more efficiently without disturbing the secondary structure by pepsin treatment. Therefore, the blacktip reef shark skin could serve as a potential source for collagen extraction for the pharmaceutical and biomedical applications. Full article

(This article belongs to the Special Issue Biomedical and Pharmacological Applications of Marine Collagen)

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17 pages, 4399 KiB

Open AccessArticle

A 3D-Printed Polycaprolactone/Marine Collagen Scaffold Reinforced with Carbonated Hydroxyapatite from Fish Bones for Bone Regeneration

by Se-Chang Kim, Seong-Yeong Heo, Gun-Woo Oh, Myunggi Yi and Won-Kyo Jung

Mar. Drugs 2022, 20(6), 344; https://0-doi-org.brum.beds.ac.uk/10.3390/md20060344 - 25 May 2022

Cited by 9 | Viewed by 3056

Abstract

In bone tissue regeneration, extracellular matrix (ECM) and bioceramics are important factors, because of their osteogenic potential and cell–matrix interactions. Surface modifications with hydrophilic material including proteins show significant potential in tissue engineering applications, because scaffolds are generally fabricated using synthetic polymers and bioceramics. In the present study, carbonated hydroxyapatite (CHA) and marine atelocollagen (MC) were extracted from the bones and skins, respectively, of Paralichthys olivaceus. The extracted CHA was characterized using Fourier transform infrared (FTIR) spectroscopy and X-ray diffraction (XRD) analysis, while MC was characterized using FTIR spectroscopy and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The scaffolds consisting of polycaprolactone (PCL), and different compositions of CHA (2.5%, 5%, and 10%) were fabricated using a three-axis plotting system and coated with 2% MC. Then, the MC3T3-E1 cells were seeded on the scaffolds to evaluate the osteogenic differentiation in vitro, and in vivo calvarial implantation of the scaffolds was performed to study bone tissue regeneration. The results of mineralization confirmed that the MC/PCL, 2.5% CHA/MC/PCL, 5% CHA/MC/PCL, and 10% CHA/MC/PCL scaffolds increased osteogenic differentiation by 302%, 858%, 970%, and 1044%, respectively, compared with pure PCL scaffolds. Consequently, these results suggest that CHA and MC obtained from byproducts of P. olivaceus are superior alternatives for land animal-derived substances. Full article

(This article belongs to the Special Issue Biomedical and Pharmacological Applications of Marine Collagen)

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Graphical abstract

16 pages, 4087 KiB

Open AccessArticle

Fish Collagen Peptides Protect against Cisplatin-Induced Cytotoxicity and Oxidative Injury by Inhibiting MAPK Signaling Pathways in Mouse Thymic Epithelial Cells

by Won Hoon Song, Hye-Yoon Kim, Ye Seon Lim, Seon Yeong Hwang, Changyong Lee, Do Young Lee, Yuseok Moon, Yong Jung Song and Sik Yoon

Mar. Drugs 2022, 20(4), 232; https://0-doi-org.brum.beds.ac.uk/10.3390/md20040232 - 28 Mar 2022

Cited by 5 | Viewed by 2450

Abstract

Thymic epithelial cells (TECs) account for the most abundant and dominant stromal component of the thymus, where T cells mature. Oxidative- or cytotoxic-stress associated injury in TECs, a significant and common problem in many clinical settings, may cause a compromised thymopoietic capacity of TECs, resulting in clinically significant immune deficiency disorders or impairment in the adaptive immune response in the body. The present study demonstrated that fish collagen peptides (FCP) increase cell viability, reduce intracellular levels of reactive oxygen species (ROS), and impede apoptosis by repressing the expression of Bax and Bad and the release of cytochrome c, and by upregulating the expression of Bcl-2 and Bcl-xL in cisplatin-treated TECs. These inhibitory effects of FCP on TEC damage occur via the suppression of ROS generation and MAPK (p38 MAPK, JNK, and ERK) activity. Taken together, our data suggest that FCP can be used as a promising protective agent against cytotoxic insults- or ROS-mediated TEC injury. Furthermore, our findings provide new insights into a therapeutic approach for the future application of FCP in the prevention and treatment of various types of oxidative- or cytotoxic stress-related cell injury in TECs as well as age-related or acute thymus involution. Full article

(This article belongs to the Special Issue Biomedical and Pharmacological Applications of Marine Collagen)

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17 pages, 3289 KiB

Open AccessArticle

A Novel Gelatinase from Marine Flocculibacter collagenilyticus SM1988: Characterization and Potential Application in Collagen Oligopeptide-Rich Hydrolysate Preparation

by Jian Li, Jun-Hui Cheng, Zhao-Jie Teng, Xia Zhang, Xiu-Lan Chen, Mei-Ling Sun, Jing-Ping Wang, Yu-Zhong Zhang, Jun-Mei Ding, Xin-Min Tian and Xi-Ying Zhang

Mar. Drugs 2022, 20(1), 48; https://0-doi-org.brum.beds.ac.uk/10.3390/md20010048 - 03 Jan 2022

Cited by 2 | Viewed by 1887

Abstract

Although the S8 family in the MEROPS database contains many peptidases, only a few S8 peptidases have been applied in the preparation of bioactive oligopeptides. Bovine bone collagen is a good source for preparing collagen oligopeptides, but has been so far rarely applied in collagen peptide preparation. Here, we characterized a novel S8 gelatinase, Aa2_1884, from marine bacterium Flocculibacter collagenilyticus SM1988^T, and evaluated its potential application in the preparation of collagen oligopeptides from bovine bone collagen. Aa2_1884 is a multimodular S8 peptidase with a distinct domain architecture from other reported peptidases. The recombinant Aa2_1884 over-expressed in Escherichia coli showed high activity toward gelatin and denatured collagens, but no activity toward natural collagens, indicating that Aa2_1884 is a gelatinase. To evaluate the potential of Aa2_1884 in the preparation of collagen oligopeptides from bovine bone collagen, three enzymatic hydrolysis parameters, hydrolysis temperature, hydrolysis time and enzyme-substrate ratio (E/S), were optimized by single factor experiments, and the optimal hydrolysis conditions were determined to be reaction at 60 ℃ for 3 h with an E/S of 400 U/g. Under these conditions, the hydrolysis efficiency of bovine bone collagen by Aa2_1884 reached 95.3%. The resultant hydrolysate contained 97.8% peptides, in which peptides with a molecular weight lower than 1000 Da and 500 Da accounted for 55.1% and 39.5%, respectively, indicating that the hydrolysate was rich in oligopeptides. These results indicate that Aa2_1884 likely has a promising potential application in the preparation of collagen oligopeptide-rich hydrolysate from bovine bone collagen, which may provide a feasible way for the high-value utilization of bovine bone collagen. Full article

(This article belongs to the Special Issue Biomedical and Pharmacological Applications of Marine Collagen)

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25 pages, 5350 KiB

Open AccessArticle

A Collagen Basketweave from the Giant Squid Mantle as a Robust Scaffold for Tissue Engineering

by Anastasia Frolova, Nadezhda Aksenova, Ivan Novikov, Aitsana Maslakova, Elvira Gafarova, Yuri Efremov, Polina Bikmulina, Vadim Elagin, Elena Istranova, Alexandr Kurkov, Anatoly Shekhter, Svetlana Kotova, Elena Zagaynova and Peter Timashev

Mar. Drugs 2021, 19(12), 679; https://0-doi-org.brum.beds.ac.uk/10.3390/md19120679 - 29 Nov 2021

Cited by 4 | Viewed by 3579

Abstract

The growing applications of tissue engineering technologies warrant the search and development of biocompatible materials with an appropriate strength and elastic moduli. Here, we have extensively studied a collagenous membrane (GSCM) separated from the mantle of the Giant squid Dosidicus Gigas in order to test its potential applicability in regenerative medicine. To establish the composition and structure of the studied material, we analyzed the GSCM by a variety of techniques, including amino acid analysis, SDS-PAGE, and FTIR. It has been shown that collagen is a main component of the GSCM. The morphology study by different microscopic techniques from nano- to microscale revealed a peculiar packing of collagen fibers forming laminae oriented at 60–90 degrees in respect to each other, which, in turn, formed layers with the thickness of several microns (a basketweave motif). The macro- and micromechanical studies showed high values of the Young’s modulus and tensile strength. No significant cytotoxicity of the studied material was found by the cytotoxicity assay. Thus, the GSCM consists of a reinforced collagen network, has high mechanical characteristics, and is non-toxic, which makes it a good candidate for the creation of a scaffold material for tissue engineering. Full article

(This article belongs to the Special Issue Biomedical and Pharmacological Applications of Marine Collagen)

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Graphical abstract

17 pages, 5747 KiB

Open AccessArticle

Preparation and Characterization of Thermally Stable Collagens from the Scales of Lizardfish (Synodus macrops)

by Junde Chen, Guangyu Wang and Yushuang Li

Mar. Drugs 2021, 19(11), 597; https://0-doi-org.brum.beds.ac.uk/10.3390/md19110597 - 21 Oct 2021

Cited by 9 | Viewed by 1904

Abstract

Marine collagen is gaining vast interest because of its high biocompatibility and lack of religious and social restrictions compared with collagen from terrestrial sources. In this study, lizardfish (Synodus macrops) scales were used to isolate acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC). Both ASC and PSC were identified as type I collagen with intact triple-helix structures by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and spectroscopy. The ASC and PSC had high amino acids of 237 residues/1000 residues and 236 residues/1000 residues, respectively. Thus, the maximum transition temperature (T_max) of ASC (43.2 °C) was higher than that of PSC (42.5 °C). Interestingly, the T_max of both ASC and PSC was higher than that of rat tail collagen (39.4 °C) and calf skin collagen (35.0 °C), the terrestrial collagen. Solubility tests showed that both ASC and PSC exhibited high solubility in the acidic pH ranges. ASC was less susceptible to the “salting out” effect compared with PSC. Both collagen types were nontoxic to HaCaT and MC3T3-E1 cells, and ASC was associated with a higher cell viability than PSC. These results indicated that ASC from lizardfish scales could be an alternative to terrestrial sources of collagen, with potential for biomedical applications. Full article

(This article belongs to the Special Issue Biomedical and Pharmacological Applications of Marine Collagen)

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Graphical abstract

26 pages, 7510 KiB

Open AccessArticle

Potential Biomedical Applications of Collagen Filaments derived from the Marine Demosponges Ircinia oros (Schmidt, 1864) and Sarcotragus foetidus (Schmidt, 1862)

by Marina Pozzolini, Eleonora Tassara, Andrea Dodero, Maila Castellano, Silvia Vicini, Sara Ferrando, Stefano Aicardi, Dario Cavallo, Marco Bertolino, Iaroslav Petrenko, Hermann Ehrlich and Marco Giovine

Mar. Drugs 2021, 19(10), 563; https://0-doi-org.brum.beds.ac.uk/10.3390/md19100563 - 06 Oct 2021

Cited by 14 | Viewed by 2701

Abstract

Collagen filaments derived from the two marine demosponges Ircinia oros and Sarcotragus foetidus were for the first time isolated, biochemically characterised and tested for their potential use in regenerative medicine. SDS-PAGE of isolated filaments revealed a main collagen subunit band of 130 kDa in both of the samples under study. DSC analysis on 2D membranes produced with collagenous sponge filaments showed higher thermal stability than commercial mammalian-derived collagen membranes. Dynamic mechanical and thermal analysis attested that the membranes obtained from filaments of S. foetidus were more resistant and stable at the rising temperature, compared to the ones derived from filaments of I. oros. Moreover, the former has higher stability in saline and in collagenase solutions and evident antioxidant activity. Conversely, their water binding capacity results were lower than that of membranes obtained from I. oros. Adhesion and proliferation tests using L929 fibroblasts and HaCaT keratinocytes resulted in a remarkable biocompatibility of both developed membrane models, and gene expression analysis showed an evident up-regulation of ECM-related genes. Finally, membranes from I. oros significantly increased type I collagen gene expression and its release in the culture medium. The findings here reported strongly suggest the biotechnological potential of these collagenous structures of poriferan origin as scaffolds for wound healing. Full article

(This article belongs to the Special Issue Biomedical and Pharmacological Applications of Marine Collagen)

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