Biomolecular Interactions at Interfaces

Interfaces play an active role in regulating biomolecular structure and function. Our research explores how peptides interact with biological and bio-inspired interfaces, including lipid membranes, nanoparticles, and soft matter surfaces. We examine how interfacial properties such as curvature, charge, and chemical functionality modulate peptide adsorption, self-assembly, and membrane activity. By elucidating interface-driven effects on peptide behavior, we aim to better understand processes such as antimicrobial activity, viral particle binding and concentration, and biomolecular transport in cellular environments.

Related Publications

^{Torsten John, Lisandra L Martin, Bernd Abel (2023). Peptide Self‐Assembly into Amyloid Fibrils at Hard and Soft Interfaces – From Corona Formation to Membrane Activity. Macromolecular Bioscience. https://doi.org/10.1002/mabi.202200576}

^{Torsten John, Stefania Piantavigna, Tiara J A Dealey, Bernd Abel, Herre Jelger Risselada, Lisandra L Martin (2023). Lipid oxidation controls peptide self-assembly near membranes through a surface attraction mechanism. Chemical Science. https://doi.org/10.1039/D3SC00159H}

^{Torsten John, Lisandra L Martin, Herre Jelger Risselada, Bernd Abel (2022). Curvature model for nanoparticle size effects on peptide fibril stability and molecular dynamics simulation data. Data in Brief. https://doi.org/10.1016/j.dib.2022.108598}

^{Torsten John, Juliane Adler, Christian Elsner, Johannes Petzold, Martin Krueger, Lisandra L Martin, Daniel Huster, Herre Jelger Risselada, Bernd Abel (2022). Mechanistic insights into the size-dependent effects of nanoparticles on inhibiting and accelerating amyloid fibril formation. Journal of Colloid and Interface Science. https://doi.org/10.1016/j.jcis.2022.04.134}

^{Torsten John, George W Greene, Nitin A Patil, Tiara J A Dealey, Mohammed A Hossain, Bernd Abel, Lisandra L Martin (2019). Adsorption of Amyloidogenic Peptides to Functionalized Surfaces Is Biased by Charge and Hydrophilicity. Langmuir. https://doi.org/10.1021/acs.langmuir.9b02063}

^{Torsten John, Tiara J A Dealey, Nicholas P Gray, Nitin A Patil, Mohammed A Hossain, Bernd Abel, John A Carver, Yuning Hong, Lisandra L Martin (2019). The Kinetics of Amyloid Fibrillar Aggregation of Uperin 3.5 Is Directed by the Peptide’s Secondary Structure. Biochemistry. https://doi.org/10.1021/acs.biochem.9b00536}

^{Torsten John, Anika Gladytz, Clemens Kubeil, Lisandra L Martin, Herre Jelger Risselada, Bernd Abel (2018). Impact of nanoparticles on amyloid peptide and protein aggregation: a review with a focus on gold nanoparticles. Nanoscale. https://doi.org/10.1039/C8NR04506B}

^{Torsten John, Bernd Abel, Lisandra L Martin (2018). The Quartz Crystal Microbalance with Dissipation Monitoring (QCM-D) Technique Applied to the Study of Membrane-Active Peptides. Australian Journal of Chemistry. https://doi.org/10.1071/CH18129}

^{Lisandra L Martin, Clemens Kubeil, Stefania Piantavigna, Tarun Tikkoo, Nicholas P Gray, Torsten John, Antonio N Calabrese, Yanqin Liu, Yuning Hong, Mohammed A Hossain, Nitin Patil, Bernd Abel, Ralf Hoffmann, John H Bowie, John A Carver (2018). Amyloid aggregation and membrane activity of the antimicrobial peptide uperin 3.5. Peptide Science. https://doi.org/10.1002/pep2.24052}