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2015
DOI: 10.1016/j.saa.2015.01.003
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Two-dimensional infrared spectroscopic study on the thermally induced structural changes of glutaraldehyde-crosslinked collagen

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Cited by 49 publications
(26 citation statements)
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“…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%
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“…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%
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“…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
confidence: 99%
“…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].…”
Section: Atr-ftir Spectra Analysismentioning
confidence: 93%