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

Subject Area Physical Chemistry of Molecules, Liquids and Interfaces, Biophysical Chemistry
Biological and Biomimetic Chemistry
Experimental Condensed Matter Physics
Statistical Physics, Nonlinear Dynamics, Complex Systems, Soft and Fluid Matter, Biological Physics
Term from 2013 to 2017
Project identifier Deutsche Forschungsgemeinschaft (DFG) - Project number 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 Programme Research Grants
 
 

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