Self-assembly characterization of tilapia skin collagen in simulated body fluid with different salt concentrations

Tian, Haohao; Ren, Zhongyang; Shi, Linfan; Hao, Gengxin; Weng, Wuyin

doi:10.1016/j.procbio.2021.06.013

Cited by 21 publications

(20 citation statements)

References 45 publications

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“…These results suggest that for grass carp collagen, pH may have a greater effect on fibril formation than salinity. We speculated that increased NaCl concentration and pH promoted the formation of collagen fibers, mainly by increasing the interaction of hydrogen bonds, which is consistent with the results of previous studies [ 38 , 39 ].…”

Section: Resultssupporting

confidence: 92%

“…Combined with the SC fibril formation results, these findings indicated that the increase in hardness, springiness, and cohesiveness at higher salinity and pH could be attributed to the strengthening of the cross-linking of SC fibrils and fibril thickening to some extent. These results are similar to those reported for tilapia SC, which is used in biomedical applications [ 39 ]. The good texture properties of SC gels indicated their potential for application in biomaterials.…”

Section: Resultssupporting

confidence: 90%

“…The amide A peak of collagen is reported to shift to a lower frequency when its N-H group participates in the formation of hydrogen bonds during collagen self-assembly [ 38 ]. The shift of other characteristic absorption peaks (amides B/III) to a lower frequency is also related to the enhancement of hydrogen bond interactions [ 39 ]. In contrast, the amino I and II peaks in SC and SBC fibrils did not show an obvious shift compared with SC and SBC.…”

Section: Resultsmentioning

confidence: 99%

“…The functional group structures and compositions of SC gels varied with the changes in salinity and pH. Compared with SC fibrils, the amide A and III peaks of SC gels appeared at lower levels and the amide B peak almost disappeared, which may be related to the formation and enhancement of hydrogen bond interactions between collagen and collagen fibril molecules [ 38 , 39 ]. The addition of genipin also promotes the intermolecular cross-linking of collagen and collagen fibrils through the formation of covalent bonds [ 16 ].…”

Section: Resultsmentioning

confidence: 99%

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Properties of Grass Carp (Ctenopharyngodon idella) Collagen and Gel for Application in Biomaterials

Shen

Zhang

et al. 2022

Gels

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The biochemical properties of collagens and gels from grass carp (Ctenopharyngodon idella) were studied to explore the feasibility of their application in biomaterials. The yields of skin collagen (SC) and swim bladder collagen (SBC) extracted from grass carp were 10.41 ± 0.67% and 6.11 ± 0.12% on a wet basis, respectively. Both collagens were characterized as type I collagen. Denaturation temperatures of SC and SBC were 37.41 ± 0.02 °C and 39.82 ± 0.06 °C, respectively. SC and SBC had high fibril formation ability in vitro, and higher values of salinity (NaCl, 0–280 mM) and pH (6–8) in formation solution were found to result in faster self-assembly of SC and SBC fibrils as well as thicker fibrils. Further tests of SC gels with regular morphology revealed that their texture properties and water content were affected by pH and NaCl concentration. The hardness, springiness, and cohesiveness of SC gels increased and the chewiness and water content decreased as pH increased from 7 to 8 and NaCl concentration increased from 140 to 280 mM. These properties suggest that collagens from grass carp may be useful in biomaterial applications in the future.

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Section: Resultssupporting

confidence: 92%

Section: Resultssupporting

confidence: 90%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 2 more Smart Citations

Properties of Grass Carp (Ctenopharyngodon idella) Collagen and Gel for Application in Biomaterials

Shen

Zhang

et al. 2022

Gels

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“…I formed fibrils diameters with a wide range ( Figs 8 and 9 ). A D-periodic cross-striated pattern is a typical characteristic of collagen fibrils obtained by self-assembly and is essential for the mechanical and biological properties of collagen-based matrices [ 28 ]. The D-periodic arrangement is also critical for the formation of heterotypic structures consisting of fibrillar collagens and other collagenous or noncollagenous macromolecules [ 29 ].…”

Section: Discussionmentioning

confidence: 99%

Extraction and characterization of bovine collagen Type V and its effects on cell behaviors

Luo

Zhang

et al. 2022

Regenerative Biomaterials

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Collagen type V (Col. V) plays an essential role in cell behaviors and has attracted increasing attention in recent years. High-purity Col. V is needed for evaluating its biological properties. In this research, the enzymatic hydrolysis process was combined with ultrafiltration to purify Col. V from the bovine cornea. The purity of Col. V was determined to be above 90.00% by both sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and high-performance liquid chromatography (HPLC) methods. The effect of Col. V on cell behaviors was evaluated. The circular dichroism (CD) spectroscopy results demonstrated that the extracted Col. V exhibited a complete triple helix structure. SDS-PAGE suggested that the molecular weight (MW) of Col. V was 440 kDa. The self-assembly experiment revealed that the proportion of Col. V in the collagen mixture can affect the Col. I fiber diameter. The cell culture results implied that Col. V can inhibit fibroblasts (L929) proliferation. The L929 showed maximum mobility when the addition of Col. V was 30%. Thus, Col. V has the effect of inhibiting L929 proliferation and promoting migration. The high-purity Col. V provides useful information for further understanding its biological implications.

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Collagen-based hydrogels induce hyaline cartilage regeneration by immunomodulation and homeostasis maintenance

Gao,

Wang,

Dai

et al. 2024

Acta Biomaterialia

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Self-assembly characterization of tilapia skin collagen in simulated body fluid with different salt concentrations

Cited by 21 publications

References 45 publications

Properties of Grass Carp (Ctenopharyngodon idella) Collagen and Gel for Application in Biomaterials

Properties of Grass Carp (Ctenopharyngodon idella) Collagen and Gel for Application in Biomaterials

Extraction and characterization of bovine collagen Type V and its effects on cell behaviors

Collagen-based hydrogels induce hyaline cartilage regeneration by immunomodulation and homeostasis maintenance

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