Recent studies have reported on the design of dynamic peptide assemblies for biomolecules encapsulation, with similar properties to those of intracellular liquid membraneless organelles. These dynamic assemblies differ from kinetically trapped or thermodynamically favorable structures in that they employ a combination of intra- and intermolecular order/disorder features. Their assembly is mainly driven by either (or combination of) electrostatic, hydrophobicor cation-πinteractions. We design and characterize peptides which self-assemble through liquid-liquid phase separation (LLPS) into dynamic structures that can compartmentalize enzymatic reactions. We use these peptide structures as simple in vitromodels of membraneless organelles to study their formation at the molecular level and the effect of environmental factors on their stability and functionality.


Lampel, A. Chem, 2020, j.chempr.2020.03.005

Ulijn, R. V. & Lampel, A. Isr. J. Chem., 2019.