Bereiche | Tage | Auswahl | Suche | Aktualisierungen | Downloads | Hilfe
CPP: Fachverband Chemische Physik und Polymerphysik
CPP 4: Crystallization, Nucleation and Self-Assembly I
CPP 4.5: Vortrag
Montag, 17. März 2025, 12:30–12:45, H34
Self-assembled Peptides Structure Mediated by Solid Interfaces — •Leila Sahebmohammadi1, Pol Besenius2, Markus Mezger3, and Regine von Klitzing1 — 1Soft Matter at Interfaces, Department of Physics, Technical University of Darmstadt, Germany — 2Department of Chemistry, Johannes Gutenberg-Universität Mainz, Germany — 3Faculty of Physics, Universität Wien, Austria
The self-assembly of amphiphilic, C3-symmetric dendritic peptides is driven by non-covalent interactions and steric limitations. This study focuses on peptides with a thermosensitive moiety. In phosphate buffer, oppositely charged peptide amphiphiles form 1D nanorod-like patterns, confirmed by circular dichroism spectroscopy to follow a ß-sheet structure. Atomic Force Microscopy (AFM) revealed temperature-dependent helical filaments, where higher temperatures increased filament length and pitch due to the hydrophobic thermosensitive moiety, while reducing filament height. Quartz Crystal Microbalance with Dissipation (QCM-D) showed a temperature-responsive, layer-by-layer adsorption process forming stable multilayers. Lysine-based cationic comonomers improved adsorption and coating uniformity on gold (Au) and silicon (Si) surfaces. Extreme pH conditions (2 or 12) caused multilayer removal, revealing a pH-responsive mechanism from weakened electrostatic interactions. This study demonstrates how self-assembly and surface confinement adapt peptide assembly, offering insights for modifying surface properties for diverse applications.
Keywords: Self-assembled peptides; Thermosensitive amphiphiles; Surface-mediated assembly; Layer-by-layer adsorption; Electrostatic assembly