کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1987136 | 1540293 | 2010 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Stabilization of collagen by cross-linking with oxazolidine E-resorcinol
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Cross-linking agents play an important part in the physical properties of collagen based biomaterials. This paper describes the stabilization of type I collagen using an oxazolidine E-resorcinol compound. It is shown by NMR and elemental analysis techniques that oxazolidine E undergoes ring opening to form an N-methylol intermediate form and then reacts with the hydrogen bonds of resorcinol. Oxazolidine E-resorcinol compound treated collagen fibers are shown by DSC analysis to be more thermally stable than simple oxazolidine E-resorcinol treated collagen. Treated collagen fibers showed shrinkage temperature around 98 °C implying that the oxazolidine E-resorcinol compounds impart thermal stability. Circular dichroism revealed that there is no major alteration in the structure of collagen after treatment with the compound. The study demonstrates that the involvement of hydrogen bonding and hydrophobic interaction as the principal mechanisms for stabilization of collagen by oxazolidine E-resorcinol compounds.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 46, Issue 5, 1 June 2010, Pages 535-539
Journal: International Journal of Biological Macromolecules - Volume 46, Issue 5, 1 June 2010, Pages 535-539
نویسندگان
Hui Chen, Zhi-hua Shana,