The effect of hydration on molecular chain mobility and the viscoelastic behavior of resilin-mimetic protein-based hydrogels.

The outstanding rubber-like elasticity of resilin and resilin-mimetic proteins depends critically on the level of hydration. In this investigation, water vapor sorption and the role of hydration on the molecular chain dynamics and viscoelastic properties of resilin-mimetic protein, rec1-resilin is investigated in detail. The dynamic and equilibrium swelling behavior of the crosslinked protein hydrogels with different crosslink density are reported under various controlled environments.

A pH-responsive interface derived from resilin-mimetic protein Rec1-resilin.

In this investigation, for the first time we report the effects of pH on the molecular orientation, packing density, structural properties, adsorption characteristics and viscoelastic behaviour of resilin-mimetic protein rec1-resilin at the solid-liquid interface using quartz crystal microbalance with dissipation monitoring (QCM-D) and surface plasmon resonance (SPR) spectroscopy. QCM-D and SPR data confirm that the binding ability of rec1-resilin on a substrate is strongly pH-dependent the protein packing density on a gold surface is calculated to be 4.45 x 10(13) per cm(2) at the isoelectric point (IEP approximately 4.

Physical approaches for fabrication of organized nanostructure of resilin-mimetic elastic protein rec1-resilin.

Protein adsorption on surfaces is a fundamental step in many applications. While various methods such as lithography, self assembly using nanoparticles, layer-by-layer attachment, etc. have been employed, here we report fabrication of controlled nanostructure of a new resilin-mimetic elastic protein rec1-resilin using physical approaches.