The paper is a carefully written review about a hot topic, the quantification of non-covalent binding interactions by mass spectrometry (MS). Although there are solution phase methods available to address such questions, MS promises to be much more sensitive and faster, and gives direct information about binding stoichiometry.

No, rather, it reviews an important new development, namely the potential of mass spectrometry to measure non-covalent binding quantitatively.

Molecules can interact by forming strong, real chemical ("covalent") bonds or by non-covalent interactions that are weaker and can easily break. Non-covalent interactions play an important role in many biochemical processes, for example signaling or protein folding. The determination of the strength of non-covalent interactions is thus important but can be tedious with conventional methods. Mass spectrometry offers a new way to study the strength of noncovalent interactions.  Our paper highlights the recent developments in this area and comprehensively reviews the literature on the topic.

This area is a niche in the application of mass spectrometry to biochemistry and biology. Sequencing of biopolymers by mass spectrometry, for example, has now become quite common and is used in industry. Measuring noncovalent interaction strength by mass spectrometry is still a very new field where there is a lot of new territory to be covered and where there are many unanswered fundamental questions that make this topic an attractive one for academic researchers.

Prof. Dr. Renato Zenobi
Laboratorium für Organische Chemie
ETH Hönggerberg, HCI
Zürich, Switzerland