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Annual Review of Analytical Chemistry

Volume 10, 2017

The Solution Assembly of Biological Molecules Using Ion Mobility Methods: From Amino Acids to Amyloid β-Protein

Abstract

Ion mobility spectrometry-mass spectrometry (IMS-MS) methods are increasingly used to study noncovalent assemblies of peptides and proteins. This review focuses on the noncovalent self-assembly of amino acids and peptides, systems at the heart of the amyloid process that play a central role in a number of devastating diseases. Three different systems are discussed in detail: the 42-residue peptide amyloid-β42 implicated in the etiology of Alzheimer's disease, several amyloid-forming peptides with 6–11 residues, and the assembly of individual amino acids. We also discuss from a more fundamental perspective the processes that determine how quickly proteins and their assemblies denature when the analyte ion has been stripped of its solvent in an IMS-MS measurement and how to soften the measurement so that biologically meaningful data can be recorded.

Keyword(s): amyloid formation, ion mobility spectrometry, mass spectrometry, protein folding, protein self-assembly
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2017-06-12
2025-06-14
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The Solution Assembly of Biological Molecules Using Ion Mobility Methods: From Amino Acids to Amyloid β-Protein
Annual Review of Analytical Chemistry 10, 365 (2017); https://doi.org/10.1146/annurev-anchem-071114-040304
/content/journals/10.1146/annurev-anchem-071114-040304
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