A new light in the assembly of intrinsically disordered peptides

Intrinsically disordered short peptides play an important role in protein function and assembly; however, their characterization and mechanism of assembly into more complicated superstructures remains a challenge. In this issue of Chem, Egelman, Wang, Xu, and co-workers employ, for the first time, cryo-electron microscopy to study the self-assembly of intrinsically disordered peptides. Intrinsically disordered short peptides play an important role in protein function and assembly; however, their characterization and mechanism of assembly into more complicated superstructures remains a challenge. In this issue of Chem, Egelman, Wang, Xu, and co-workers employ, for the first time, cryo-electron microscopy to study the self-assembly of intrinsically disordered peptides. Hierarchical assembly of intrinsically disordered short peptidesGuo et al.ChemMay 16, 2023In BriefCyro-EM reveals that aromatic packing from pyrenes enables the assemblies of intrinsically disordered peptides (IDPs), and subsequently, molecular engineering indicates that interfibrillar interactions create hierarchical assemblies. As the first example of atomistic structures of IDP assemblies, this work provides new insights to design the assemblies of IDPs and to understand the disorder-to-order transition in small molecule self-assembly in water. Full-Text PDF