Abstract
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.
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