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Related Experiment Video

Updated: Jul 5, 2025

Standards for Quantitative Metalloproteomic Analysis Using Size Exclusion ICP-MS

Standards for Quantitative Metalloproteomic Analysis Using Size Exclusion ICP-MS

Published on: April 13, 2016

Recent Advances in Metalloproteomics.

James P C Coverdale¹, Sirilata Polepalli², Marco A Z Arruda³

¹School of Pharmacy, Institute of Clinical Sciences, University of Birmingham, Edgbaston B15 2TT, UK.

|January 23, 2024

Summary

Understanding metalloproteomes is crucial for life sciences. This review explores new methods and challenges in studying protein-metal interactions, focusing on labile essential and toxic metals.

Keywords:

essential metals ligand exchange kinetics metallodrugs metalloproteome xenobiotic metals

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Last Updated: Jul 5, 2025

Standards for Quantitative Metalloproteomic Analysis Using Size Exclusion ICP-MS

Standards for Quantitative Metalloproteomic Analysis Using Size Exclusion ICP-MS

Published on: April 13, 2016

Optimized Protocol for the Extraction of Proteins from the Human Mitral Valve

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Published on: June 14, 2017

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

Area of Science:

Biochemistry
Metallomics
Proteomics

Background:

Protein-metal interactions are vital in physiology, medicine, and toxicology.
Metalloproteomes are complex and often ill-defined due to labile metal-protein complexes.
Challenges exist in analyzing interactions involving essential, toxic, and xenobiotic metals.

Purpose of the Study:

To review recent advances in studying protein-metal interactions across (sub-)proteomes.
To discuss challenges in analyzing labile metal ion complexes.
To examine transition metal interactions, including metallodrug-protein complexes.

Main Methods:

Review of recently developed analytical approaches.
Focus on separation techniques adapted to metal reactivity.
Examination of methods for studying labile and inert metal complexes.

Main Results:

Metalloproteomes remain challenging to define due to complex interactions.
New approaches are emerging for studying labile and inert metal-protein complexes.
Separation strategies must be tailored to specific metal ion properties.

Conclusions:

Accurate characterization of metalloproteomes requires advanced analytical techniques.
Understanding protein-metal interactions is key to advancements in medicine and toxicology.
Further research into tailored separation methods is essential for metalloproteomics.