کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10574209 | 976519 | 2006 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Stabilization of type I collagen against collagenases (type I) and thermal degradation using iron complex
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی معدنی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The widespread application of collagen as a biomaterial warrants research in understanding the stabilization of the same. In this study, interaction of iron-tetrakis (hydroxymethyl) phosphonium (THP) complex with type I collagen has been investigated. DSC and hydrothermal measurement studies reveal that the shrinkage temperature of iron-THP treated rat tail tendon (RTT) collagen is 33 °C higher than that of native RTT collagen. Fe-THP complex also brings about high degree of enzymatic stability to type I collagen. The effect of Fe-THP on the conformation of collagen was studied using circular dichroism and it was found that no major alterations in the triple helical structure of collagen occur on treatment with Fe-THP. It is observed from viscosity experiment results that though Fe-THP complex is able to bring about long range ordering of collagen, as evident from the thermal and enzymatic stability imparted to collagen, this ordering does not lead to any aggregation of collagen. Since THPS is reducing in nature, it is expected to keep iron in the +2 state and if THP chelates to Fe(II), the hydrolytic behavior of iron can also be controlled.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Inorganic Biochemistry - Volume 100, Issue 11, November 2006, Pages 1774-1780
Journal: Journal of Inorganic Biochemistry - Volume 100, Issue 11, November 2006, Pages 1774-1780
نویسندگان
Nishtar Nishad Fathima, Murugan Chandra Bose, Jonnalagadda Raghava Rao, Balachandran Unni Nair,