
Dr. Max Lallemang
Institute of Physical Chemistry
University of Freiburg
Project
AFM based characterization of fuel-driven materials
Project description
Life is far from equilibrium: It is fuelled by constant energy dissipation, which is regulated via a feedback mechanism. Active and adaptive molecular systems use chemicals to fuel their structures in a dissipative steady-state. Once the energy is spent, the system relaxes and returns to the ground state. This results in transient steady states with unusual dynamics, adaptability and autonomous system lifetimes. My objective is to use an atomic force microscope (AFM) to characterize non-equilibrium materials systems across time and length scales.
Project outcomes
DNA and peptide structures are programmable and show promise for creating materials that can respond and adapt. Unlike traditional materials, which try to stay in equilibrium, these new materials are designed to constantly interact with their environment.
To study these structures, we used the Atomic Force Microscope (AFM). In order to monitor and investigate dynamic processes and rupture forces of single molecules at the nanoscale and mesoscale, imaging and single molecule force spectroscopy (SMFS) are used. Here, we started with simple responsive systems at the nanoscale and later on, we moved towards complex responsive systems at the nanoscale and macroscale, compromising molecular fuel.
We investigated how DNA interacts with different ions in solutions. We found that the strength of the interaction depends on the type of ion. We also studied how different types of bonds contribute to the strength of materials. By understanding these bonds, we hope to create materials with stronger adhesion.
Furthermore we studied how certain proteins and molecules affect the formation of amyloid-beta fibrils, which are related to Alzheimer's disease. By understanding this process, we hope to learn more about the disease.
Additionally, we studied how DNA can be put together and taken apart using special enzymes and fuel. We also looked at how amino acids can assemble into peptides and larger structures. These studies help us to understand how materials can be built from the ground up.
Lastly, we designed a hydrogel from a single DNA hairpin. We also showed how this structure can respond to different triggers. This research opens up possibilities for creating new materials that can adapt and generate their own energy.
Overall, this research is paving the way for the development of innovative materials made of DNA and peptides. These materials have the potential to be active, adaptive, and self-sustaining. By studying their behavior and interactions, we hope to create materials that can be used in various applications.
Supervisor and Dissertation
Prof. Dr. Thorsten Hugel
Max Lallemang completed his dissertation in April 2023.
Dissertation: AFM based characterization of fuel-driven materials
Current employer
Max Lallemang currently works at the Lycée Hubert-Clément Esch/Alzette in Luxembourg.
Publications in livMatS
- Angle-dependent strength of a single chemical bond by stereographic force spectroscopy*
Cai, W., Bullerjahn, J. T., Lallemang, M., Kroy, K., Balzer, B. N., & Hugel, T. (2022). Angle-dependent strength of a single chemical bond by stereographic force spectroscopy. Chemical Science. doi: 10.1039/D2SC01077A - Study of repellence on polymeric surfaces with two individually adjustable pore hierarchies*
Goralczyk, A., Zhu, M., Mayoussi, F., Lallemang, M., Tschaikowsky, M., Warmbold, A., Caliaro, S., Tauber, F., Balzer, B. N., Kotz-Helmer, F., Helmer, D., & Rapp, B. E. (2022). Study of repellence on polymeric surfaces with two individually adjustable pore hierarchies. Chemical Engineering Journal, 437, 135287. doi: 10.1016/j.cej.2022.135287 - Multivalent non-covalent interactions lead to strongest polymer adhesion*
Lallemang, M., Yu, L., Cai, W., Rischka, K., Hartwig, A., Haag, R., Hugel, T., and Balzer, B. N. (2022). Multivalent non-covalent interactions lead to strongest polymer adhesion. Nanoscale. doi: 10.1039/d1nr08338d - ATP Impedes the Inhibitory Effect of Hsp90 on Aβ40 Fibrillation*
Wang, H., Lallemang, M., Hermann, B., Wallin, C., Loch, R., Blanc, A., Balzer, B. N., Hugel, T., & Luo, J. (2020). ATP impedes the inhibitory effect of Hsp90 on Aβ40 fibrillation. Journal of Molecular Biology. doi: 10.1016/j.jmb.2020.11.016
* Funded by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany's Excellence Strategy – EXC-2193/1 – 390951807