Meeting Abstract

4.2  Tuesday, Jan. 4  Dynamic mechanical properties of a mimetic muscle protein DUDEK, DM*; LV, S; CAO, Y; BALAMURALI, MM; GOSLINE, JG; LI, H; Virginia Tech; Univ of British Columbia; Univ of British Columbia; Univ of British Columbia; Univ of British Columbia; Univ of British Columbia dmdudek@vt.edu

The passive mechanical properties of muscle are dominated by the elastic protein, titin, a complex molecular spring composed of folded immunoglobulin-like domains interspaced with short unstructured domains. This molecular structure provides macroscopic samples of muscle with their unique combination of strength, extensibility, and resilience. We have reproduced these properties in a chimeric synthetic protein composed of folded GB1 domains from yeast and short, unstructured sequences of resilin from fruit flies. In quasi-static tests, these biomaterials act as resilient springs at low strains and shock absorbing dampers at high strains, mimicking the properties of titin. When subjected to small amplitude oscillations, these materials showed frequency independent stiffness and resilience independent of the initial pre-strain, suggesting that the dynamic properties are governed by the unfolded regions of the protein. The mechanical properties of these biomaterials can be fine-tuned by adjusting the relative compositions of GB1 and resilin, providing the opportunity to develop biomaterials that are mimetic of different types of muscles. We anticipate that these biomaterials will find applications in tissue engineering as scaffold and matrix for artificial muscles.