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

Benjamin Gabriel Poulson, Kacper Szczepski, Joanna Izabela Lachowicz, Lukasz Jaremko, Abdul-Hamid M. Emwas, Mariusz Jaremko

Research output: Contribution to journalArticlepeer-review

69 Scopus citations

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.
Original languageEnglish (US)
Pages (from-to)215-227
Number of pages13
JournalRSC Advances
Volume10
Issue number1
DOIs
StatePublished - 2020

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01
Acknowledgements: The authors would like to thank King Abdullah University of Science and Technology (KAUST) for financial support.

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