Development and characterization of a photo-cross-linked functionalized type-I collagen (Oreochromis niloticus) and polyethylene glycol diacrylate hydrogel

Bao, Zixian; Gao, Minghong; Fan, Xiying; Cui, Yanshan; Yang, Junqing; Peng, Xinying; Xian, Mo; Sun, Yue; Nian, Rui

doi:10.1016/j.ijbiomac.2020.03.210

Cited by 20 publications

(12 citation statements)

References 51 publications

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“…The surface structures of films were examined using an SEM (S-4800, Hitachi, Japan). The acceleration voltage was set to 5.0 kV …”

Section: Methodsmentioning

confidence: 99%

“…Measurements were performed in aluminum oxide pans under a nitrogen atmosphere (20 mL min −1 ) at a heating rate of 20 °C min −1 from 50 to 800 °C. 32 2.6. Mechanical Properties.…”

Section: Characterization Of Masp1mentioning

confidence: 99%

“…At a predetermined time (days 1, 3, and 7), 10% (v/v) CCK-8 solution (Vazyme, Nanjing, China) was added into the culture medium and incubated for 2 h. The absorbance of the culture medium was recorded at 450 nm using a Spark 10 M microplate reader (Tecan, Switzerland). 32 For cell staining, cells were washed with PBS to remove FBS and cultured in DMEM/F-12 with 1,1′-dioctadecy1-3,3,3′,3′-tetramethylindocarbocyanine perchlorate (10 μg mL −1 , DiI, Sigma-Aldrich, USA). Cells were then successively incubated at 37 °C for 5 min and 4 °C for 15 min followed by washing twice with PBS before the addition of complete cell culture medium.…”

Section: Characterization Of Masp1mentioning

confidence: 99%

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High-Strength Collagen-Based Composite Films Regulated by Water-Soluble Recombinant Spider Silk Proteins and Water Annealing

Peng

Cui

Chen

et al. 2022

ACS Biomater. Sci. Eng.

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Spider silk has attracted extensive attention in the development of high-performance tissue engineering materials because of its excellent physical properties, biocompatibility, and biodegradability. Although high-molecular-weight recombinant spider silk proteins can be obtained through metabolic engineering of host bacteria, the solubility of the recombinant protein products is always poor. Strong denaturants and organic solvents have thus had to be exploited for their dissolution, and this seriously limits the applications of recombinant spider silk protein-based composite biomaterials. Herein, through adjusting the temperature, ionic strength, and denaturation time during the refolding process, we successfully prepared water-soluble recombinant spider major ampullate spidroin 1 (sMaSp1) with different repeat modules (24mer, 48mer, 72mer, and 96mer). Then, MaSp1 was introduced into the collagen matrix for fabricating MaSp1-collagen composite films. The introduction of spider silk proteins was demonstrated to clearly alter the internal structure of the composite films and improve the mechanical properties of the collagen-based films and turn the opaque protein films into transparency ones. More interestingly, the composite film prepared with sMaSp1 exhibited better performance in mechanical strength and cell adhesion compared to that prepared with water-insoluble MaSp1 (pMaSp1), which might be attributed to the effect of the initial dissolved state of MaSp1 on the microstructure of composite films. Additionally, the molecular weight of MaSp1 was also shown to significantly influence the mechanical strength (enhanced to 1.1-to 2.3-fold) and cell adhesion of composite films, and 72mer of sMaSp1 showed the best physical properties with good bioactivity. This study provides a method to produce recombinant spider silk protein with excellent water solubility, making it possible to utilize this protein under environmentally benign, mild conditions. This paves the way for the application of recombinant spider silk proteins in the development of diverse composite biomaterials.

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“…The surface structures of films were examined using an SEM (S-4800, Hitachi, Japan). The acceleration voltage was set to 5.0 kV …”

Section: Methodsmentioning

confidence: 99%

“…Measurements were performed in aluminum oxide pans under a nitrogen atmosphere (20 mL min −1 ) at a heating rate of 20 °C min −1 from 50 to 800 °C. 32 2.6. Mechanical Properties.…”

Section: Characterization Of Masp1mentioning

confidence: 99%

Section: Characterization Of Masp1mentioning

confidence: 99%

See 1 more Smart Citation

High-Strength Collagen-Based Composite Films Regulated by Water-Soluble Recombinant Spider Silk Proteins and Water Annealing

Peng

Cui

Chen

et al. 2022

ACS Biomater. Sci. Eng.

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“…Collagen has already been extracted and characterised for a broad range of marine species including jellyfish [36,37], cuttlefish [38], sea sponges [39,40], and numerous fishes [32][33][34][35][41][42][43][44][45][46]. In a handful of studies, marine collagen has also successfully been methacrylated to form collagen or gelatin methacrylate [20,26,47,48]. Given that an estimated 50% of commercial fish weight is currently discarded as non-consumable waste [49], fish industry by-products offer an economical and environmentally sustainable source of collagen.…”

Section: Introductionmentioning

confidence: 99%

“…To our knowledge however, investigations into the potential use of marine collagens as biomaterials for neural cell 3D tissue engineering has so far been limited to a study showing differentiation of induced pluripotent (iPS) cells to the specific lineage of dorsal cortical neurons in collagen extracted from the fish species Tilapia [54]. With respect to methacrylated marine gelatin or collagen, the only work that has been reported has been with fibroblast cells [20,26,47]. We aimed to assess the potential for methacrylated collagen from the common fish, Red Snapper, to be used as a biomaterial for 3D bioprinting of neural cells.…”

Section: Introductionmentioning

confidence: 99%

Light Cross-Linkable Marine Collagen for Coaxial Printing of a 3D Model of Neuromuscular Junction Formation

et al. 2020

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Collagen is a major component of the extracellular matrix (ECM) that modulates cell adhesion, growth, and migration, and has been utilised in tissue engineering applications. However, the common terrestrial sources of collagen carry the risk of zoonotic disease transmission and there are religious barriers to the use of bovine and porcine products in many cultures. Marine based collagens offer an attractive alternative and have so far been under-utilized for use as biomaterials for tissue engineering. Marine collagen can be extracted from fish waste products, therefore industry by-products offer an economical and environmentally sustainable source of collagen. In a handful of studies, marine collagen has successfully been methacrylated to form collagen methacrylate (ColMA). Our work included the extraction, characterization and methacrylation of Red Snapper collagen, optimisation of conditions for neural cell seeding and encapsulation using the unmodified collagen, thermally cross-linked, and the methacrylated collagen with UV-induced cross-linking. Finally, the 3D co-axial printing of neural and skeletal muscle cell cultures as a model for neuromuscular junction (NMJ) formation was investigated. Overall, the results of this study show great potential for a novel NMJ in vitro 3D bioprinted model that, with further development, could provide a low-cost, customizable, scalable and quick-to-print platform for drug screening and to study neuromuscular junction physiology and pathogenesis.

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Proteins and Polypeptides as Biomaterials Inks for 3D Printing

Hajiabbas

Okoro

Delporte

et al. 2023

Handbook of the Extracellular Matrix

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Development and characterization of a photo-cross-linked functionalized type-I collagen (Oreochromis niloticus) and polyethylene glycol diacrylate hydrogel

Cited by 20 publications

References 51 publications

High-Strength Collagen-Based Composite Films Regulated by Water-Soluble Recombinant Spider Silk Proteins and Water Annealing

High-Strength Collagen-Based Composite Films Regulated by Water-Soluble Recombinant Spider Silk Proteins and Water Annealing

Light Cross-Linkable Marine Collagen for Coaxial Printing of a 3D Model of Neuromuscular Junction Formation

Proteins and Polypeptides as Biomaterials Inks for 3D Printing

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