Serial in situ SANS study of disordered protein-graphene oxide (GO) co-assembling complex

Elastin-like recombinamers (ELRs) are recombinant disordered proteins that exhibit a reversible-phase transition with a change in temperature. A hybrid solid gel-like structure generates at the interface of an ELR and GO solution at ELR’s transition temperature (Tt). SANS has been used to elucidate the underlying ELR-GO molecular interaction mechanism and co-assembling hybrid complex. Recently, we have found another type of similar disordered protein, Resilin, which can also generate gel with GO. Resilin also exhibits a reversible-phase transition in temperature. However, the specific aggregate geometry and interaction mechanism of GO and Resilin are not clear. It is important to characterize the average co-assembling size and volume percent of Resilin-GO compared with ELR-GO and understand the underlying mechanism to develop a series of disordered protein-GO systems by using SANS.