2D Interfacial Crystallization Stabilized by Short-Chain Aliphatic Interfaces.

ABSTRACT: We report the discovery and in-depth investigation of interfacial crystallization (IFC), the assembly and formation of membrane-like crystalline sheets from both chiral amino acid and achiral N-substituted glycine "peptoid" amide monomers selectively at vapor-liquid and liquid-liquid interfaces. This is the first assembly process known to be shared by two peptidomimic families of molecules with crucial backbone differences. A series of AFM, SEM, TOF-SIMS, FTIR, X-ray crystallography, counterion screening experiments, QM calculations, and MD simulation studies identified that IFC is based on the assembly of single monomer layers with alternating molecular orientations, which results in bilayers of unit thickness 1.2-1.6 nm consisting of internal hydrophobic planes and ionic interface

SUBMITTER: Swanson HWA 

PROVIDER: S-EPMC11948478 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature