Characterization of resilin-like proteins with tunable mechanical properties.

Abstract

Resilin is an elastomeric protein abundant in insect cuticle. Its exceptional properties, which include high resilience and efficient energy storage, motivate its potential use in tissue engineering and drug delivery applications. Our lab has previously developed recombinant proteins based on the resilin-like sequence derived from Anopheles gambiae and demonstrated their promise as a scaffold for cartilage and vascular engineering. In this work, we describe a more thorough investigation of the physical properties of crosslinked resilin-like hydrogels. The resilin-like proteins rapidly form crosslinked hydrogels in physiological conditions. We also show that the mechanical properties of these resilin-like hydrogels can be modulated simply by varying the protein concentration or the stoichiometric ratio of crosslinker to crosslinking sites. Crosslinked resilin-like hydrogels were hydrophilic and had a high water content when swollen. In addition, these hydrogels exhibited moderate resilience values, which were comparable to those of common synthetic rubbers. Cryo-scanning electron microscopy showed that the crosslinked resilin-like hydrogels at 16 wt% featured a honeycomb-like structure. These studies thus demonstrate the potential to use recombinant resilin-like proteins in a wide variety of applications such as tissue engineering and drug delivery due to their tunable physical properties.