Biomedical

Recent Advances in Metalloproteomics







  Peer Reviewed

Abstract

Interactions between proteins and metal ions and their complexes are important in many areas of the life sciences, including physiology, medicine, and toxicology. Despite the involvement of essential elements in all major processes necessary for sustaining life, metalloproteomes remain ill-defined. This is not only owing to the complexity of metalloproteomes, but also to the non-covalent character of the complexes that most essential metals form, which complicates analysis. Similar issues may also be encountered for some toxic metals. The review discusses recently developed approaches and current challenges for the study of interactions involving entire (sub-)proteomes with such labile metal ions. In the second part, transition metals from the fourth and fifth periods are examined, most of which are xenobiotic and also tend to form more stable and/or inert complexes. A large research area in this respect concerns metallodrug–protein interactions. Particular attention is paid to separation approaches, as these need to be adapted to the reactivity of the metal under consideration.

Key Questions about Metalloproteomics

The article "Recent Advances in Metalloproteomics" provides an overview of the interactions between proteins and metal ions, which are crucial in various biological processes, including physiology, medicine, and toxicology. Despite the essential role of metal ions in sustaining life, the study of metalloproteomes has been challenging due to their complexity and the non-covalent nature of many metal-protein interactions. The review discusses recent methodologies and ongoing challenges in analyzing these interactions, with a particular focus on transition metals from the fourth and fifth periods, many of which are xenobiotic and form stable complexes. The authors also highlight the significance of metallodrug–protein interactions and emphasize the need for specialized separation techniques tailored to the reactivity of specific metals.

1. What are metalloproteomes, and why are they significant in biological systems?

Metalloproteomes refer to the complete set of metalloproteins within a cell or organism. These proteins contain metal ions as cofactors, which are essential for various biological functions, including enzyme catalysis, electron transport, and signal transduction. Understanding metalloproteomes is crucial for comprehending the full scope of cellular processes and the impact of metal ions on health and disease.

2. What challenges are associated with studying metalloproteomes?

The study of metalloproteomes is complicated by the complexity of metal-protein interactions and the non-covalent nature of many of these complexes. This complexity makes it difficult to analyze and characterize metalloproteins accurately. Additionally, the presence of labile metal ions and the dynamic nature of metal binding further complicate the study of metalloproteomes.

3. How do transition metals from the fourth and fifth periods influence metalloproteomics?

Transition metals from the fourth and fifth periods, many of which are xenobiotic, tend to form more stable and inert complexes. These stable complexes can have significant biological effects, including interactions with proteins and nucleic acids. Understanding these interactions is essential for elucidating the mechanisms of action of metallodrugs and the potential toxicological effects of these metals.

4. What are metallodrug–protein interactions, and why are they important?

Metallodrug–protein interactions involve the binding of metal-containing drugs to proteins, which can modulate protein function and influence therapeutic outcomes. These interactions are important because they can lead to the development of new therapeutic agents and provide insights into the mechanisms of action of existing metallodrugs. Understanding these interactions is also crucial for assessing the safety and efficacy of metal-based therapies.

5. What specialized separation techniques are necessary for studying metalloproteomes?

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