The secrets of life lie in the molecular flexibility.

Welcome to Prof. Mariusz Jaremko's research group, the

Flexible Systems Lab!

Our research group works mainly on metabolites which are important for human health, and our current main focus in this discipline is oriented towards food, food safety, food quality, and food fraud by utilizing state-of-the-art instrumentation in metabolomics studies. We are also working on aggregation of amylin, a biological peptide that is connected tightly with diabetes II, a disease that is closely related to unhealthy diets. So, food science and the consequences of the food we eat are one of the main areas which the group Flexible Systems investigates. We are also working to develop methods and pulse programs in Nuclear Magnetic Resonance (NMR) that allow us to uncover obscured metabolites and to detect them at lower concentrations, in order to understand metabolic pathways better. 


Why the name Flexible Systems?

It's simple; because metabolites, as well as amylin and its analogues, are very flexible systems i.e. amylin does not have a defined 3D structure, and in the case of the small molecules and metabolites we study, while they do have defined structures, they often exhibit very high levels of dynamic flexibility due to their size.

Untangling untidy folds to understand diseases

Copper ions could play a key role when peptide folding goes wrong and leads to harmful aggregates.

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Picking the best methods for metabolomics research

Comparison of different nuclear magnetic resonance spectroscopy methods has helped to identify the most robust approach for studying different types of biomolecules.

Latest Publications

Aggregation of biologically important peptides and proteins: inhibition or acceleration depending on protein and metal ion concentrations

by Benjamin Gabriel Poulson, Kacper Szczepski, Joanna Izabela Lachowicz, Lukasz Jaremko, Abdul-Hamid Emwas, Mariusz Jaremko
Review Article Year: 2020 DOI: https://doi.org/10.1039/C9RA09350H

Abstract

The process of aggregation of proteins and peptides is dependent on the concentration of proteins, and the rate of aggregation can be altered by the presence of metal ions, but this dependence is not always a straightforward relationship. In general, aggregation does not occur under normal physiological conditions, yet it can be induced in the presence of certain metal ions. However, the extent of the influence of metal ion interactions on protein aggregation has not yet been fully comprehended. A consensus has thus been difficult to reach because the acceleration/inhibition of the aggregation of proteins in the presence of metal ions depends on several factors such as pH and the concentration of the aggregated proteins involved as well as metal concentration level of metal ions. Metal ions, like Cu2+, Zn2+, Pb2+ etc. may either accelerate or inhibit aggregation simply because the experimental conditions affect the behavior of biomolecules. It is clear that understanding the relationship between metal ion concentration and protein aggregation will prove useful for future scientific applications. This review focuses on the dependence of the aggregation of selected important biomolecules (peptides and proteins) on metal ion concentrations. We review proteins that are prone to aggregation, the result of which can cause serious neurodegenerative disorders. Furthering our understanding of the relationship between metal ion concentration and protein aggregation will prove useful for future scientific applications, such as finding therapies for neurodegenerative diseases.