Researcher(s)
- Arriana Bisram, , University of Delaware
Faculty Mentor(s)
- Kristi Kiick, biomedical engineering, material science and engineering, University of Delaware
Abstract
Biomimetic, peptide-based materials have received attention for their usage in biomedical applications due to their display of biocompatibility, tunability, and cost efficiency in comparison to synthetic materials. One such peptide-based material which is of interest is resilin-like polypeptides. Resilin is an elastomeric protein derived from insects that demonstrates stimuli responsiveness and elasticity, and has been a point of inspiration for the creation of resilin-like polypeptides (RLPs) based on the CG15920 gene segment of the fruit fly Drosophila melanogaster. This RLP can be conjugated with a coiled-coiled bundlemer forming peptide, which results in the formation of programmable constructs that are responsive to stimuli such as pH, temperature, and chemical environment. This work aims to express and characterize the propensity for phase separation of RLP-functionalized coiled-coil constructs with various central amino acid substitutions in the resilin unit. To yield the desired protein sequence, recombinant synthesis was utilized and followed by denaturing purification. The protein was then analyzed using MALDI-TOF MS in order to characterize the molecular weight and purity of produced constructs. Afterward, UV-vis was used in order to investigate the phase behavior of the constructs at different concentrations in response to temperature. The optical density at 350 nanometers was observed with regard to temperature, allowing us to find the point of phase transition. Results of this investigation displayed that intermolecular interactions have a significant impact on the phase transition behavior of constructs.