Physicochemical characterization and self-assembly of human amniotic membrane and umbilical cord collagen: A comparative study

Gunasekaran, Deebasuganya; Thada, Rajarajeshwari; Jeyakumar, Grace Felciya Sekar; Manimegalai, Nivethitha Panneerselvam; Shanmugam, Ganesh; Uma, T.

doi:10.1016/j.ijbiomac.2020.10.107

Cited by 13 publications

(7 citation statements)

References 47 publications

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“…Collagen molecules possess all the information needed for fibrillogenesis so that it could self-assemble to be high-ordered fibrils when exposed to physiological conditions [ 2 ]. The collagen turbidimetric curve ( Figure 1 A) generally comprised three distinct stages to be a sigmoidal profile: lag phase (nucleation stage), growth phase (assembly stage) and plateau phase (equilibrium stage), indicating that the kinetics of collagen fibrillation followed a nucleation-dependent polymerization mechanism [ 15 ].…”

Section: Resultsmentioning

confidence: 99%

“…Mechanisms of D-periodicity formation are still not well-understood, but ultrasonic treatment may affect the length of gap areas and overlapping areas through variable molecular arrangement, resulting in the smaller D-periodicities according to the 1/4 staggered model of Schmitt hypothesis [ 19 , 29 ]. The collagen fibrils with smaller diameter interact more affine with ECM components, facilitating elasticity and decreased plastic deformation [ 2 ]. The uniform morphology of collagen fibrils (diameter size distributions, network structure, etc.)…”

Section: Resultsmentioning

confidence: 99%

“…Collagen is the predominant structural protein of extracellular matrix (ECM), constituting approximately 1/3 of the total body proteins [ 1 ]. Type I collagen (CI) is the most abundant amongst the identified 29 collagen types (type I–XXIX), and also possess superior biodegradability and biocompatibility, which has now been widely utilized in food, cosmetics, biomedical and pharmaceutical industries [ 2 , 3 ]. Whether in vivo or in vitro under physiological conditions (specific pH, temperature, ionic strength, concentration, etc.…”

Section: Introductionmentioning

confidence: 99%

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Impact of Ultrasonication on the Self-Assembly Behavior and Gel Properties of Bovine Bone Collagen I

et al. 2023

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This study deliberated the effect of ultrasonic treatment on collagen self-assembly behavior and collagen fibril gel properties. Bovine bone collagen I which had undergone ultrasonic treatment with different power (0–400 W) and duration (0–60 min) was analyzed. SDS-PAGE and spectroscopic analysis revealed that ultrasonic treatment decreased collagen molecular order degree and the number of hydrogen bonds, stretching collagen telopeptide regions while maintaining the integrity of the collagen triple-helical structure. Ultrasonic treatment (p ≤ 200 W, t ≤ 15 min) dispersed the collagen aggregates more evenly, and accelerated collagen self-assembly rate with a decreased but more homogeneous fibril diameter (82.78 ± 16.47–115.52 ± 19.51 nm) and D-periodicity lengths (62.1 ± 2.9–66.5 ± 1.8 nm) than that of the untreated collagen (119.15 ± 27.89 nm; 66.5 ± 1.8 nm). Meanwhile, ultrasonic treatment (p ≤ 200 W, t ≤ 15 min) decreased the viscoelasticity index and gel strength, enhancing thermal stability and promoting specific surface area and porosity of collagen fibril gels than that of the untreated collagen fibril gel. These results testified that collagen self-assembly behavior and collagen fibril gel properties can be regulated by ultrasonic treatment through multi-hierarchical structural alteration. This study provided a new approach for controlling in vitro collagen fibrillogenesis process so as to manufacture novel desirable collagen-based biomaterials with propitious performances for further valorization.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Impact of Ultrasonication on the Self-Assembly Behavior and Gel Properties of Bovine Bone Collagen I

et al. 2023

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“…For the collagen-based solid samples, the porosity and fibrillary structure would enhance cell adherence and proliferation. Generally, the homogeneous pore structure provides a suitable environment for the adhesion, proliferation, migration of cells and formation of new tissues [ 12 ]. Differences in morphology may have different biological effects.…”

Section: Resultsmentioning

confidence: 99%

“…In this study, a collagen extraction process was investigated. Col. V makes up 10–20% of the fibril-forming collagens in the corneal stroma [ 12 ]. It was adopted as the raw materials for collagen extraction based on a combination of acid-enzymatic hydrolysis and membrane separation.…”

Section: Introductionmentioning

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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Biomimetic Mineralized Collagen Scaffolds for Bone Tissue Engineering: Strategies on Elaborate Fabrication for Bioactivity Improvement

Wu,

Li,

Wang

et al. 2024

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Biomimetic mineralized collagen (BMC) scaffolds represent an innovative class of bone‐repair biomaterials inspired by the natural biomineralization process in bone tissue. Owing to their favorable biocompatibility and mechanical properties, BMC scaffolds have garnered significant attention in bone tissue engineering. However, most studies have overlooked the importance of bioactivity, resulting in collagen scaffolds with suboptimal osteogenic potential. In this review, the composition of the mineralized extracellular matrix (ECM) in bone tissue is discussed to provide guidance for biomimetic collagen mineralization. Subsequently, according to the detailed fabrication procedure of BMC scaffolds, the substances that can regulate both the fabrication process and biological activities is summarized. Furthermore, a potential strategy for developing BMC scaffolds with superior mechanical properties and biological activities for bone tissue engineering is proposed.

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Physicochemical characterization and self-assembly of human amniotic membrane and umbilical cord collagen: A comparative study

Cited by 13 publications

References 47 publications

Impact of Ultrasonication on the Self-Assembly Behavior and Gel Properties of Bovine Bone Collagen I

Impact of Ultrasonication on the Self-Assembly Behavior and Gel Properties of Bovine Bone Collagen I

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

Biomimetic Mineralized Collagen Scaffolds for Bone Tissue Engineering: Strategies on Elaborate Fabrication for Bioactivity Improvement

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