Abstract
Native mass spectrometry (MS) involves the analysis and characterization of macromolecules, predominantly intact proteins and protein complexes, whereby as much as possible the native structural features of the analytes are retained. As such, native MS enables the study of secondary, tertiary, and even quaternary structure of proteins and other biomolecules. Native MS represents a relatively recent addition to the analytical toolbox of mass spectrometry and has over the past decade experienced immense growth, especially in enhancing sensitivity and resolving power but also in ease of use. With the advent of dedicated mass analyzers, sample preparation and separation approaches, targeted fragmentation techniques, and software solutions, the number of practitioners and novel applications has risen in both academia and industry. This review focuses on recent developments, particularly in high-resolution native MS, describing applications in the structural analysis of protein assemblies, proteoform profiling of-among others-biopharmaceuticals and plasma proteins, and quantitative and qualitative analysis of protein-ligand interactions, with the latter covering lipid, drug, and carbohydrate molecules, to name a few.
| Original language | English |
|---|---|
| Pages (from-to) | 7269–7326 |
| Journal | Chemical Reviews |
| Volume | 122 |
| Issue number | 8 |
| Early online date | 20 Aug 2021 |
| DOIs | |
| Publication status | Published - 27 Apr 2022 |
Bibliographical note
Funding Information:Since its conception about 30 years ago, the research field of native MS has grown steadily, which by now has led to a rather substantial and lively research community. We acknowledge all involved, making this a scientifically competitive but very friendly and cooperative community. We acknowledge all of the researchers whose work has made it possible for us to write this comprehensive review. We apologize for missing contributions made by others; the field has grown so much that it is rather difficult to be all-inclusive. We thank all of the members of the Heck lab for their support in writing this review and for executing some of the work described in it, and we also thank all of our collaborators over the years for supplying interesting research questions and precious samples. A.J.R.H. acknowledges support from The Netherlands Organization for Scientific Research (NWO) through the Spinoza Award (SPI.2017.028). M.A.d.B. and A.J.R.H. were additionally supported by NWO NACTAR Project 16442.
Publisher Copyright:
© 2021 The Authors. Published by American Chemical Society.