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

Using NMR spectroscopy to investigate the role played by copper in prion diseases

by Rawiah Alsiary, Mawadda Alghrably, Abdelhamid Saoudi, Suliman Al-Ghamdi, Lukasz Jaremko, Mariusz Jaremko, Abdul-Hamid Emwas
Original Article Year: 2020 DOI: http://dx.doi.org/10.1007/s10072-020-04321-9

Abstract

Prion diseases are a group of rare neurodegenerative disorders that develop as a result of the conformational conversion of normal prion protein (PrPC) to the disease-associated isoform (PrPSc). The mechanism that actually causes disease remains unclear. However, the mechanism underlying the conformational transformation of prion protein is partially understood—in particular, there is strong evidence that copper ions play a significant functional role in prion proteins and in their conformational conversion. Various models of the interaction of copper ions with prion proteins have been proposed for the Cu (II)-binding, cell-surface glycoprotein known as prion protein (PrP). Changes in the concentration of copper ions in the brain have been associated with prion diseases and there is strong evidence that copper plays a significant functional role in the conformational conversion of PrP. Nevertheless, because copper ions have been shown to have both a positive and negative effect on prion disease onset, the role played by Cu (II) ions in these diseases remains a topic of debate. Because of the unique properties of paramagnetic Cu (II) ions in the magnetic field, their interactions with PrP can be tracked even at single atom resolution using nuclear magnetic resonance (NMR) spectroscopy. Various NMR approaches have been utilized to study the kinetic, thermodynamic, and structural properties of Cu (II)-PrP interactions. Here, we highlight the different models of copper interactions with PrP with particular focus on studies that use NMR spectroscopy to investigate the role played by copper ions in prion diseases.