Effects of Cr3+ on the structure of collagen fiber.
We have investigated the effects of Cr3+ on the hierarchical structure of pigskin collagen fibers by use of scanning electron microscopy (SEM), X-ray photoelectron spectroscopy (XPS), wide-angle X-ray diffraction (WAXD), confocal laser micro-Raman spectroscopy (CLRS), and circular dichroism (CD). Our results demonstrate that the introduction of Cr3+ leads to the formation of a cluster of 20-40 nm between collagen fibrils, while the unique axial periodic structure (D periodicity) of the fibrils does not change. As the Cr3+ concentration increases, the order of intermolecular lateral packing, crystallite structure within helical chains, and N and C telopeptide regions decrease. The present study reveals that Cr3+ only cross-links with collagen but does not disrupt its triple helical structure.
Wu
Bo
B
Department of Pharmaceutics and Bioengineering, National Engineering Laboratory for Clean Technology of Leather Manufacture, Sichuan University, Chengdu, Sichuan, China.
Mu
Changdao
C
Zhang
Guangzhao
G
Lin
Wei
W
D000818:Animals; D002857:Chromium / Q000378:metabolism / Q000494:pharmacology*; D003094:Collagen / Q000737:chemistry* / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D008855:Microscopy, Electron, Scanning; D013057:Spectrum Analysis; D013329:Structure-Activity Relationship; D014961:X-Ray Diffraction
D002857:Chromium; D003094:Collagen