At the Biomolecular Systems and Design Lab, we focus on understanding and engineering the dynamic behavior of biomolecules in complex environments. Our research sits at the interface of biophysical and computational chemistry, where we integrate experimental techniques and theoretical models to reveal the fundamental principles of biomolecular interactions and self-assembly. This molecular-level insight is crucial for advancing the design of bionanomaterials.

By investigating how biomolecules assemble and interact—both in solution and at interfaces such as membranes and nanoparticles—we aim to drive innovations in areas like neurodegenerative diseases, nanomedicine, viral infection, and antimicrobial strategies.

Research Focus

• Self-Assembly: Understanding the mechanisms of peptide self-assembly with an emphasis on the bio-nano-interface.
• Membrane Interactions: Studying peptide behavior in biomimetic membranes to inform novel strategies for antimicrobial activity and viral infection.
• Bionanomaterials: Designing peptide fibrils and the surface properties of viral-like particles for biomedical applications.

Our group leverages a synergy of theory and experiment, using computational chemistry to guide experimental design and gain a deeper understanding of biomolecular systems.

• Physical Chemistry (Fall & Spring, CO-440)

• Physical Chemistry Lab (Spring, CO-446-B)

Hayn, M.; John, T.; Bandak, J.; Rauch‐Wirth, L.; Abel, B.; Münch, J. Hybrid Materials From Peptide Nanofibrils and Magnetic Beads to Concentrate and Isolate Virus Particles. Adv. Funct. Mater. 2024, 34 (27), 2316260. 
DOI: https://doi.org/10.1002/adfm.202316260

John, T.; Rampioni, A.; Poger, D.; Mark, A. E. Molecular Insights into the Dynamics of Amyloid Fibril Growth: Elongation and Lateral Assembly of GNNQQNY Protofibrils. ACS Chem. Neurosci. 2024. 15 (4), 716–723.
DOI: https://doi.org/10.1021/acschemneuro.3c00754

John, T.; Piantavigna, S.; Dealey, T. J. A.; Abel, B.; Risselada, H. J.; Martin, L. L. Lipid Oxidation Controls Peptide Self-Assembly near Membranes through a Surface Attraction Mechanism. Chem. Sci. 2023, 14 (14), 3730–3741. 
DOI: https://doi.org/10.1039/D3SC00159H

John, T.; Adler, J.; Elsner, C.; Petzold, J.; Krueger, M.; Martin, L. L.; Huster, D.; Risselada, H. J.; Abel, B. Mechanistic Insights into the Size-Dependent Effects of Nanoparticles on Inhibiting and Accelerating Amyloid Fibril Formation. J. Colloid Interface Sci. 2022, 622, 804–818. 
DOI: https://doi.org/10.1016/j.jcis.2022.04.134

Jun, H.; Wang, X.; Parsons, M. F.; Bricker, W. P.; John, T.; Li, S.; Jackson, S.; Chiu, W.; Bathe, M. Rapid Prototyping of Arbitrary 2D and 3D Wireframe DNA Origami. Nucleic Acids Res. 2021, 49 (18), 10265–10274. 
DOI: https://doi.org/10.1093/nar/gkab762

John, T.; Gladytz, A.; Kubeil, C.; Martin, L. L.; Risselada, H. J.; Abel, B. Impact of Nanoparticles on Amyloid Peptide and Protein Aggregation: A Review with a Focus on Gold Nanoparticles. Nanoscale 2018, 10 (45), 20894–20913. 
DOI: https://doi.org/10.1039/C8NR04506B