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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 3: Crystallization, Nucleation and Self-Assembly I
CPP 3.10: Talk
Monday, March 18, 2024, 12:15–12:30, H 0110
Self-assembled Peptides Structure Mediated by Solid Interfaces — •Leila Sahebmohammadi1, Regine von Klitzing1, Markus Mezger2, and Pol Besenius3 — 1Soft Matter at Interfaces, Department of Physics, Technical University of Darmstadt, Germany — 2Faculty of Physics, Universität Wien, Austria — 3Department of Chemistry, Johannes Gutenberg-Universität Mainz, Germany
This study investigates the self-assembly dynamics of thermosensitive amphiphilic dendritic C3-symmetric peptides containing lysine and glutamic acid, respectively. Using Quartz Crystal Microbalance with Dissipation (QCM-D) techniques, our observations reveal temperature-dependent layer-by-layer adsorption of the oppositely charged peptides, achieving the formation of multilayers. Atomic Force Microscopy (AFM) substantiates these findings, providing visual confirmation of the confinement distribution pattern on the surface. Simultaneously, a strategic combination of supramolecular assembly and surface confinement is explored using QCM techniques.
Lysine emerges as the optimal grafting layer, exhibiting heightened adsorption on gold (Au) and silicon (Si) surfaces. Further QCM-D investigations show the same growth increment for the oppositely charged peptides at pH 6.5. Notably, exposure to extreme pH conditions (2 or 12) induces the removal of multilayers, due to low charge density of one of the peptides. This results in a better understanding of peptide self-assembly and insights for customizing surface properties through combining self-assembly and surface confinement.
Keywords: self assembly, QCM-D, Peptides, Isoelectric point