Multi-scale characterization of thermoresponsive dendritic elastin-like peptides.

Elastin like peptides (ELPs)-polypeptides based on the protein elastin-are used widely as thermoresponsive components in biomaterials due to the presence of a sharp soluble-to-insoluble phase change at a characteristic transition temperature (T). While linear ELPs have been thoroughly studied, few investigations into branched ELPs have been carried out. Using lysine amino acids as branching and terminal units with 1-3 pentameric repeats between each branch, ELP dendrimers were prepared by solid-phase peptide synthesis with molecular weights as high as 14kDa. A conformation change from random coil to β-turn upon heating through the T, typical of ELPs, was observed by circular dichroism spectroscopy for all peptides. The high molecular weights of these peptides enabled the use of characterization techniques typically reserved for polymers. Variable-temperature small-angle X-ray scattering measurements in dilute solution revealed an increase in size and fractal dimension upon heating, even well below the T. These results were corroborated by cryogenic transmission electron microscopy, which confirmed the presence of aggregates below the T, and micro differential scanning calorimetry, which showed a broad endothermic peak below the T. These results collectively indicate the presence of a pre-coacervation step in the phase transition of ELP dendrimers.