Abstract
Elastin-like polypeptides (ELPs) are polypentapeptides that undergo hydrophobic collapse and aggregation above a specific transition temperature, Tt . ELP diblocks sharing a common "core" block (I60) but varying "outer" blocks (A80, P40) were designed, where Tt,I < Tt,A < Tt,P . The formation of ∼55 nm diameter mixed micelles from these ELP diblocks was verified using dynamic light scattering (DLS), multiangle light scattering (MALS) and fluorescence resonance energy transfer (FRET). To confer affinity to the blood circulating protein fibrinogen, a fibrinogen-binding tetrapeptide sequence (GPRP) was fused to A80-I60, while P40-I60 was fused to a non-binding control (GPSP). The self-assembling, peptide-displaying, mixed micelles exhibit temperature-modulated avidities for immobilized and soluble fibrinogen at 32 °C and 42 °C. In this initial proof-of-concept design, the engineered mixed micelles were shown to disengage fibrinogen at elevated temperatures. The modular nature of this system can be used for developing in vivo depot systems that will only be triggered to release in situ upon specific stimuli.