Kinetics and morphology of self-assembly of an elastin-like polypeptide based on the alternating domain arrangement of human tropoelastin.

Elastin is the polymeric extracellular matrix protein responsible for the properties of extensibility and elastic recoil in tissues such as arterial blood vessels, lung parenchyma, and skin. Both tropoelastin (TE), the full-length monomeric form of elastin, and elastin-like polypeptides (ELPs), based on sequences and domain arrangements of TE, have the intrinsic ability to undergo organized self-assembly into network structures through a process of temperature-induced phase separation or coacervation. It has been suggested that this property plays a role in in vivo formation of the extracellular elastic matrix. In general, the temperature at which phase separation takes place has been taken as the measure of propensity for self-assembly. However, this phase separation is only the first step in a more complex, multistep process of network formation. We have previously shown that analysis of spectrophotometric data allows extraction of kinetic parameters describing both early (coacervation) and later (maturation) steps of the self-assembly process. Here, using a well-characterized ELP containing three hydrophobic domains flanking two cross-linking domains, we describe the effects of temperature, polypeptide concentration, and solution conditions on the kinetics of self-assembly, providing insights into possible mechanisms for the spontaneous organization of such ELPs into extended networks.