Stabilization of collagen by cross-linking with oxazolidine E-resorcinol

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.