title: 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.
authors.affiliation: Department of Chemistry and Biochemistry, Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306; email: cbleiholder@fsu.edu.
authors.forename: Christian
authors.initials: C
authors.lastname: Bleiholder
authors.affiliation: Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106.
authors.forename: Michael T
authors.initials: MT
authors.lastname: Bowers
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism / Q000473:pathology; D000596:Amino Acids / Q000737:chemistry* / Q000378:metabolism; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D007477:Ions / Q000737:chemistry; D018625:Microscopy, Atomic Force; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D021241:Spectrometry, Mass, Electrospray Ionization
chemical_list: D000596:Amino Acids; D016229:Amyloid beta-Peptides; D007477:Ions; D010455:Peptides
keywords: amyloid formation; ion mobility spectrometry; mass spectrometry; protein folding; protein self-assembly