Materials World Network: Fundamentals of Peptide Materials - Experimental and Simulation Probes

• Antragsteller: Professor Dr. Markus Valtiner
• Fachliche Zuordnung: Physikalische Chemie von Molekülen, Flüssigkeiten und Grenzflächen, Biophysikalische Chemie ; Biologische und Biomimetische Chemie ; Experimentelle Physik der kondensierten Materie ; Statistische Physik, Nichtlineare Dynamik, Komplexe Systeme, Weiche und fluide Materie, Biologische Physik
• Förderung: Förderung von 2013 bis 2017
• Projektkennung: Deutsche Forschungsgemeinschaft (DFG) - Projektnummer 238994672

Peptides have emerged as an important class of biocompatible, environmentally friendly, sustainable material alternatives. On the one hand, they can be engineered to self-assemble into a broad array of nanostructures important as tissue scaffolds, biosensors, drug delivery agents, and sacrificial templates for inorganic materials. On the other, they offer unique ways to modify solid interfaces with surface protecting, hydrophobic, antibiotic, or adhesive capabilities. However, their rational engineering is limited by lack of a detailed understanding of the ways in which their many distinct molecular interactions - hydrogen bonding, electrostatic, and hydrophobic forces, for example - act in concert or competition to produce complex, cooperative, many-body collective behavior. This study combines state-of-the-art atomic force microscopy (AFM) hand-in-hand with advanced molecular simulation studies to obtain innovative fundamental insights into peptide-peptide interactions and, in particular, their ability to mediate interactions at solid/liquid interfaces. Using a uniquely flexible model peptide repeat scaffold, precisely controllable sequences and numbers of interacting peptides will be examined, whereby interactions and cooperativities can be tuned with exacting control. Detailed AFM measurements will be compared to molecular pictures developed by equilibrium, quantitative all-atom simulations that probe true underlying, equilibrium interaction landscapes. In particular, the balance between hydrophobic and charge interactions and the effect of cooperative, multi-peptide interactions will be studied in a systematic and hierarchical manner.

• DFG-Verfahren: Sachbeihilfen