Interaction of Intrinsically Disordered Peptide Amphiphiles

  Tamara Ehm [1,2]  ,  Hila Shinhar [1]  ,  Roy Beck [1]  
[1] The School of Physics and Astronomy, The Center for Nanoscience and Nanotechnology, and the Center for Physics and Chemistry of Living Systems, Tel Aviv University, Israel
[2] Faculty of Physics and Center for NanoScience, Ludwig-Maximilians-Universit√§t, M√ľnchen, Germany

Intrinsically disordered proteins (IDPs) are peptide chains that do not fold into secondary or ternary structures. IDPs are common in nature and are known to interact nonspecifically with multiple partners, including themselves. We study the structures and interactions of IDP sequences conjugated to hydrophobic domains. Such molecules, termed intrinsically disordered peptide amphiphiles (IDPAs), have only recently been introduced. Due to their amphiphilic nature, IDPAs are expected to spontaneously form nanoscopic mesophases in aqueous solution. We use small angle X-ray scattering (SAXS) and cryogenic electron microscopy to investigate the pH-induced structural changes of IDPAs. I have recently shown that a small change in IDPA can lead to a significant change in their self-assembly. This allows us to extract information about the interparticle interactions of IDPs.a