title: [Specific interaction study in collagen/hyaluronic acid blends by two-dimensional infrared correlation spectroscopy].
abstract: Conformational changes and specific interactions in the collagen/hyaluronic acid blends were studied by two-dimensional infrared correlation spectroscopy with the interruption of the component of hyaluronic acid in collagen/ hyaluronic acid blends. It was found that the synchronous cross-peaks, derived from stretching vibrations of C=O at 1 694 cm(-1), wagging of N-H at 1 524 cm(-1) and in-plane deformation of N-H at 1 241 cm(-1) of collagen, were indicative of local conformational changes of collagen. The synchronous negative cross-peak between stretching vibrations of C-OH of hyaluronic acid at 1 045 cm(-1) and streching vibrations of C=O of collagen at 1 694 cm(-1) suggested that the interaction of hydrogen bonding existing between O-H of HA and C=O of collagen with the content of HA varied from 0% to 50%. With the content of HA more than 50%, the cross-peak at 1 045 cm(-1) disappeared in synchronous correlation spectra while the intensity of cross-peak at (1 694, 1 524), (1 694, 1 241), (1 524, 1 241) increased, which indicated that no interaction was found between O-H of HA and collagen, however, the interactions of hydrogen bonding existed between C=O of HA and N-H of collagen, resulting in the conformational changes of collagen.
authors.affiliation: National Engineering Laboratory for Clean Technology of Leather Manufacture, Sichuan University, Chengdu 610065, China.
authors.forename: Qing-Tian
authors.initials: QT
authors.lastname: Tan
authors.forename: Zhen-Hua
authors.initials: ZH
authors.lastname: Tian
authors.forename: Guo-Ying
authors.initials: GY
authors.lastname: Li
mesh_terms: D003094:Collagen / Q000737:chemistry*; D006820:Hyaluronic Acid / Q000737:chemistry*; D006860:Hydrogen Bonding; D013055:Spectrophotometry, Infrared; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D006820:Hyaluronic Acid; D003094:Collagen