Characterizing metal-biomolecule interactions by mass spectrometry
Samuel E Janisse1, Rebeca L Fernandez1, Marie C Heffern1
1Department of Chemistry, University of California, Davis, One Shields Drive, Davis, CA 95616, USA.
Trends in Biochemical Sciences
|July 11, 2023
Summary
Understanding metal micronutrient dynamics is crucial for health. This review highlights mass spectrometry methods for studying labile metal-biomolecule interactions in human biology.
Area of Science:
- Biochemistry
- Analytical Chemistry
- Human Biology
Background:
- Metal micronutrients are vital for organismal health, requiring a precise balance.
- The dynamic interactions between metals and biomolecules are complex and poorly understood.
- These interactions influence various physiological and pathological processes.
Purpose of the Study:
- To review the challenges in studying labile metals within biological systems.
- To highlight the utility of mass spectrometry (MS)-based approaches for investigating metal-biomolecule interactions.
- To advance the understanding of metal homeostasis and its role in health and disease.
Main Methods:
- Review of existing literature on metal-biomolecule interactions.
- Focus on mass spectrometry (MS) techniques and their applications.
- Discussion of challenges in analyzing labile metal species in biological matrices.
Main Results:
- Labile metal-biomolecule interactions are difficult to study due to their transient nature.
- Mass spectrometry offers powerful tools for identifying metal binders and characterizing metal-mediated structural changes.
- Advancements in MS enable the study of metal dynamics in both intracellular and extracellular environments.
Conclusions:
- Overcoming the challenges in studying labile metals is key to understanding their biological roles.
- Mass spectrometry-based methods are instrumental in elucidating metal-biomolecule interactions.
- Improved understanding of these interactions can lead to insights into health and disease mechanisms.
Related Concept Videos
01:19Mass Spectrometry: Overview
5.4K
Mass spectrometry is an analytical technique used to determine the molecular mass and molecular formula of a compound. The basic principle of mass spectrometry is to generate ions from the analyte molecule and measure these ion abundances against their molecular mass. One common type of ionization, known as electrospray ionization or EI, bombards the analyte molecules in the gas phase with high-energy electron beams. The electron beams displace an electron from the molecule and leave...
5.4K
01:21Mass Spectrometry: Complex Analysis
828
Mass spectrometry is an important technique for the identification of pure compounds. However, it has some limitations for the analysis of complex mixtures, often due to excessive fragmentation making the spectrum too complicated to decipher. Mass spectrometry can be combined with suitable separation methods in sequence, forming hyphenated methods, which are useful in the analysis of complex mixtures.
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...
828
01:16Mass Spectrometers
5.7K
This lesson details the instrumentation of a mass spectrometer—a physical instrument to perform mass spectrometry on analyte molecules and record the characteristic mass spectra. This is achieved via three chief functions:
5.7K
01:33Peptide Identification Using Tandem Mass Spectrometry
6.6K
Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
6.6K
01:20Mass Spectrometry: Molecular Fragmentation Overview
3.3K
The ionization of a molecule into a molecular ion inside the mass spectrometer causes instability in the molecule's structure due to the loss of an electron. This eventually leads to the fragmentation or breaking of some bonds in the molecule. The fragmentation occurs predominantly at specific bonds to yield relatively stable fragments.
One type of fragmentation pattern is the cleavage of a single bond in the molecular ion. The cleavage leads to a radical and a cation. The cleavage can...
One type of fragmentation pattern is the cleavage of a single bond in the molecular ion. The cleavage leads to a radical and a cation. The cleavage can...
3.3K
01:15High-Resolution Mass Spectrometry (HRMS)
1.4K
The resolution of a mass spectrometer depends on the efficiency of separating ions with different ion masses. The mass of an atom is approximated to the sum of the masses of protons and neutrons inside, considering the masses of protons and neutrons as equal. However, the masses of the proton (1.6726 × 10−24 g) and neutron (1.6749 × 10−24 g) are not truly equal. There is a minor error in the expression of atomic masses relative to the simplest atom of hydrogen. For...
1.4K