“…Both sol-gel and hydrogel transition temperatures then affected the collagen fibril networks as macroscopic changes. The thermal properties of collagen materials were already reported by other groups [11][12][13][17][18][19]. Although the denaturation temperature was dependent in the sample conditions such as the water content, our results are not inconsistent with previous reports.…”
Section: Discussionsupporting
confidence: 76%
“…First, the higher order structure of the AuNP-embedded collagen gels was examined using FTIR spectroscopy. The characteristic collagen signals derived from amide A (3328 cm −1 ), amide B (3084 cm −1 ), amide I (1655 cm −1 ), amide II (1555 cm −1 ), and amide III (1240 cm −1 ) are known [16,17]. These signals were observed in the AuNP-embedded collagen gels ( Figure 3).…”
Section: Thermal Denaturation Of Different Collagen Gelsmentioning
confidence: 94%
“…Thus, different discrete absorptions in amide III were observed around 1200 cm −1 [16]. The denaturation by heating of the collagen triple helix structures formed in collagen can be monitored by taking the ratio of amide III/1455 cm −1 [17,18]. The average values of 1235 cm −1 /1455 cm −1 of Cellmatrix type I-A, Atelocell IAC, and Cellmatrix type I-C before heating were 1.4, 1.3 and 1.2, respectively, and no obvious changes of the ratio were observed after heating.…”
Section: Thermal Denaturation Of Different Collagen Gelsmentioning
Cell Separation is important in various biomedical fields. We have prepared gold nanoparticle (AuNP)-embedded collagen gels as a visible-light-responsive cell scaffold in which photoinduced single cell detachment occurs through local thermal denaturation of the collagen gel via the photothermal effect of AuNP. Physicochemical properties of collagen materials depend on the origin of the collagen and the presence of telopeptides. In this study, we prepared various AuNP-embedded collagen gels by using different collagen materials with and without the telopeptides to compare their thermal denaturation properties and photoinduced single cell detachment behaviors. Cellmatrix type I-C without telopeptides exhibited a lower denaturation temperature than Cellmatrix type I-A and Atelocell IAC, as examined by Fourier transform infrared (FTIR) spectroscopy, rheological analysis, and sol–gel transition observation. Three-dimensional (3D) laser microscopic imaging revealed that collagen fibers shrank in Cellmatrix type I-A upon heating, but collagen fibers disappeared in Cellmatrix type I-C upon heating. Cells cultured on the Cellmatrix type I-C-based AuNP-embedded collagen gel detached with shorter photoirradiation than on the Cellmatrix type I-A-based AuNP-embedded collagen gel, suggesting that collagen gels without telopeptides are suitable for a photoinduced single cell detachment system.
“…Both sol-gel and hydrogel transition temperatures then affected the collagen fibril networks as macroscopic changes. The thermal properties of collagen materials were already reported by other groups [11][12][13][17][18][19]. Although the denaturation temperature was dependent in the sample conditions such as the water content, our results are not inconsistent with previous reports.…”
Section: Discussionsupporting
confidence: 76%
“…First, the higher order structure of the AuNP-embedded collagen gels was examined using FTIR spectroscopy. The characteristic collagen signals derived from amide A (3328 cm −1 ), amide B (3084 cm −1 ), amide I (1655 cm −1 ), amide II (1555 cm −1 ), and amide III (1240 cm −1 ) are known [16,17]. These signals were observed in the AuNP-embedded collagen gels ( Figure 3).…”
Section: Thermal Denaturation Of Different Collagen Gelsmentioning
confidence: 94%
“…Thus, different discrete absorptions in amide III were observed around 1200 cm −1 [16]. The denaturation by heating of the collagen triple helix structures formed in collagen can be monitored by taking the ratio of amide III/1455 cm −1 [17,18]. The average values of 1235 cm −1 /1455 cm −1 of Cellmatrix type I-A, Atelocell IAC, and Cellmatrix type I-C before heating were 1.4, 1.3 and 1.2, respectively, and no obvious changes of the ratio were observed after heating.…”
Section: Thermal Denaturation Of Different Collagen Gelsmentioning
Cell Separation is important in various biomedical fields. We have prepared gold nanoparticle (AuNP)-embedded collagen gels as a visible-light-responsive cell scaffold in which photoinduced single cell detachment occurs through local thermal denaturation of the collagen gel via the photothermal effect of AuNP. Physicochemical properties of collagen materials depend on the origin of the collagen and the presence of telopeptides. In this study, we prepared various AuNP-embedded collagen gels by using different collagen materials with and without the telopeptides to compare their thermal denaturation properties and photoinduced single cell detachment behaviors. Cellmatrix type I-C without telopeptides exhibited a lower denaturation temperature than Cellmatrix type I-A and Atelocell IAC, as examined by Fourier transform infrared (FTIR) spectroscopy, rheological analysis, and sol–gel transition observation. Three-dimensional (3D) laser microscopic imaging revealed that collagen fibers shrank in Cellmatrix type I-A upon heating, but collagen fibers disappeared in Cellmatrix type I-C upon heating. Cells cultured on the Cellmatrix type I-C-based AuNP-embedded collagen gel detached with shorter photoirradiation than on the Cellmatrix type I-A-based AuNP-embedded collagen gel, suggesting that collagen gels without telopeptides are suitable for a photoinduced single cell detachment system.
“…The amide I band curves of MGA and SGA were nearly unshifted compared with fresh MF and SF, indicating that the second structure of collagen was not destroyed. 32,33 When collagen is crosslinked with GA, the peak absorbance of the amide III bands increases. 34 On account of the formation of amide bonds between carboxyl groups and available amino groups in ME and SE, the peak of wave numbers at 1,402 cm -1 (the symmetric stretching of carboxylate salts), 1,074 cm -1 (ester bond), and 2,969 cm -1 (CH 2 bond) decreased.…”
Section: Chemical and Structural Characterization Of Cross-linked Memmentioning
Purpose: A promising vascular scaffold must possess satisfying mechanical properties, great hemocompatibility, and favorable tissue regeneration. Combining natural with synthetic materials is a popular method of creating/enhancing such scaffolds. However, the effect of additional modification on the materials requires further exploration. Materials and methods: We selected polycaprolactone (PCL), which has excellent mechanical properties and biocompatibility and can be combined with collagen. Electrospun fibers created using a PCL/collagen solution were used to fashion mixed nanofibers, while separate syringes of PCL and collagen were used to create separated nanofibers, resulting in different pore sizes. Mixed and separated nanofibers were cross-linked with glutaraldehyde (GA), 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC), and genipin; hence, we named them as mixed GA, mixed EDC (ME), mixed genipin (MG), separated GA, separated EDC (SE), and separated genipin (SG). Results: Fourier transform infrared (FTIR) spectroscopy and X-ray diffraction showed that cross-linking did not affect the main functional groups of fibers in all groups. ME, MG, SE, and SG met the requisite mechanical properties, and they also resisted collagenase degradation. In hemocompatibility assays, only ME and MG demonstrated ideal safety. Furthermore, ME and MG presented the greatest cytocompatibility. For vascular scaffolds, rapid endothelialization helps to prevent thrombosis. According to human umbilical vein endothelial cell migration on different nanofibers, ME and MG are also successful in promoting cell migration. Conclusion: ME and MG may be promising candidates for vascular tissue engineering. The study suggests that collagen cross-linked by EDC/N-hydroxysuccinimide or genipin facilitates endothelial cell regeneration, which could be of great benefit in tissue engineering of vascular scaffolds.
“…The condensation reaction of aldehyde groups in GA and protein amino groups occurred with a decrease in the number of N H groups, and correspondingly the N H bending vibration and C N stretching vibration coupling strength was reduced. This change could prove that the cross-linking reaction had happened in the EW [37][38][39].…”
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