Journal
LANGMUIR
Volume 25, Issue 19, Pages 11905-11910Publisher
AMER CHEMICAL SOC
DOI: 10.1021/la901577j
Keywords
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Funding
- National Natural Science Foundation (NNSF) of China [20704028]
- Program for New Century Excellent Talents in University [NCET-06-0788]
- Ministry of Science and Technology of China [2007CB936401]
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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.
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