Elastin is a stable and resilient protein that undergoes large deformations under low force. In the arterial tree, elastin allows the arterial wall to expand and recover as high-pressured blood is pumped from the heart. In addition, elastin stores elastic-strain energy, allowing arteries to smooth the pulsatile flow of blood from the heart, lowering peak BP, and the mechanical work of the heart. As a material, elastin is extremely durable, capable of undergoing over a billion cycles under normal hemostatic conditions, and because of its resiliency, is an attractive scaffolding material for tissue engineering applications. Aging of elastic tissue may be attributed to changes in the cross-linking of the polypeptide chain caused by biochemical processes such as oxidation and glycation, and mechanical fatigue. Little research has been done to understand the effects of biochemical changes through oxidation and glycation on the cyclic loading response of arterial elastin. Fatigue testing of materials has shown that mechanical properties such as modulus, residual and ultimate strength change with increasing number of cycles.

The work presented in this research examines the effects of glycation and oxidation on the structural and cyclic loading response of isolated arterial elastin. Two models, a linear and a Neo-Hookean model, were employed to evaluate the change in the mechanical response of arteries due to chemical glycation, oxidation and cyclic loading. While the linear model provided a better fit to our data, both models identified significant differences between treatment groups and number of cycles. In addition, this study investigated a damage model that could quantitatively detect changes in the cyclic loading response that could be attributed to fatigue damage. Although the models used in this study were able to detect changes due to cyclic loading and oxidation treatment, more work needs to be done to develop better models for the study of the cyclic loading response of isolated arterial elastin