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- W2358953906 abstract "Alkali-solubilized collagen solution cross-linked with N-hydroxysuccinimide activated adipic acid(NHS-AA) ester.The effect of NHS-AA on the secondary structure of alkali-solubilized collagen was examined.The infrared bands,determined by the Fourier-transform infrared spectroscopy(FT-IR),did not reflect characteristics which were caused the amount of cross-linking,but the results from two-dimensional infrared correlation spectroscopy(2D-IR) indicated that the positive synchronous cross-peaks,derived from stretching vibrations of C=O at 1672cm-1,C—N stretching vibrations and wagging of N—H at 1554cm-1 and in plane deformation of N—H at 1241cm-1 of collagen,were indicative of local conformational changes of collagen with increasing cross-linking.The order of secondary structure changes of cross-linked collagen was amide Ⅲ than amide Ⅰ than amide Ⅱ than —CH3 than —CH—.It was shown that the microcosmic information of a change in dynamic structure could be provided for cross-linked collagen with the interruption of the cross-linker concentration.These fundamental data should provide available information for understanding of the relationship between the structure and function of cross-linked collagen." @default.
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- W2358953906 date "2012-01-01" @default.
- W2358953906 modified "2023-09-22" @default.
- W2358953906 title "Effect of cross-linking on the conformation of collagen by two-dimensional infrared correlation spectroscopy" @default.
- W2358953906 hasPublicationYear "2012" @default.
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