Temperature induced conformational changes in the elastin-like peptide GVG(VPGVG).

Elastin-like peptides are biopolymers that display LCST behaviour in solution quite similar to other synthetic polymers like polyethylene oxide. Here we study the structure of the peptide GVG(VPGVG)3 in a temperature range of 25 °C to 70 °C with small angle neutron scattering. The LCST for this peptide is outside the experimental range of temperatures. Molecular conformation is well described within the model of a random coil but increasing temperature leads to significant changes. The peptide displays a combination of conformational change and aggregation that show up in the scattering at low and intermediate scattering vector q. The aggregate size is determined from an integral measure of the scattered intensity. It increases with temperature and concentration. For low concentration we find a size variation with temperature that may be related to the collapse of conformation at the inverse temperature transition (ITT).