Co-assembly and self-sorting are not mutually exclusive in enantiomeric peptide systems
Year: 2026
Type: article
Abstract: Co-assembly and self-sorting in multicomponent systems are typically treated as mutually exclusive outcomes. Here, we show that this distinction is incomplete. Using enantiomeric peptide nanotubes, we demonstrate that a single co-assembled structure forms only at an equimolar composition, yet remains internally self-sorted into compositionally distinct domains. Contrast-matched neutron scattering directly reveals this segregation and shows that the co-assembled structures adopt layered architectures rather than simple molecular-level mixing. These results establish that co-assembly and self-sorting can coexist within a single supramolecular object across length scales, providing a general framework for understanding and controlling multicomponent self-assembly.
Source: Chemical Science
DOI: 10.1039/d6sc04454a
Language: English
Subfield: Biomaterials
Field: Materials Science
Domain: Physical Sciences
Open Access status: diamond
Funders: National Science Foundation, University of Virginia, Government of the United Kingdom, Royal Academy of Engineering, University of Glasgow, National Institutes of Health, Engineering and Physical Sciences Research Council, Science and Technology Facilities Council, National Institute of General Medical Sciences, Division of Materials Research, National Center for Research Resources, ISIS Neutron and Muon Source
Awards: G1440776884, G1689194922, G2486305925, 300 keV Liquid Helium Robotic Microscope, G3460432961, G3537589354, Molecular Electron Microscopy Core Facility Improvements, G377745559, G4491422769, G4707408251, G5369305972, G583082977, UVA molecular electron microscopy core for the Mid-Atlantic region, G6271517897, IMR-MIP DANSE - Distributed Data Analysis for Neutron Scattering Experiments - CNST, G8546139093, Cryo-EM of Helical Protein and Nucleoprotein Polymers at Near Atomic Resolution
OpenAlex ID: W7204494351