Intrinsically disordered proteins (IDPs) are proteins that lack ordered three-dimensional structures. Many IDP`s undergo transitions to more ordered states upon binding to their targets or after exposure to suitable stimuli. Understanding synthetic IDPs assemblies and their triggered structural changes in response to different stimuli can provide relevant and important insights into the principles that govern morphological changes of naturally IDP assemblies.1
Therefore, we synthesized amphiphilic hybrids based on a short hydrophilic IDP and a hydrophobic dendron. These IDP-dendron hybrids were self-assembled in aqueous medium into supramolecular micellar structures. These structures were characterized using fluorescence spectroscopy, dynamic light scattering and small angle x-ray scattering. We varied the hydrophobic dendron and the peptide sequence to get better understanding on the relationship between the monomeric structure and morphology of the assembled state. Furthermore, we used different triggers and characterized their effect on the assembled structures.