Supramolecular assembly

Supramolecular chemistry

Materials science

Chromatography

Glycoprotein

Biochemistry

Molecule

Molecular recognition

Nanotechnology

Organic chemistry

Glycan

Characterization (materials science)

Selected reaction monitoring

Mass spectrometry

Chemistry

Ion-mobility spectrometry–mass spectrometry

Host–guest chemistry

Biomolecule

Ion-mobility spectrometry

Tandem mass spectrometry

Nature Reviews Chemistry

Despite their structural and functional differences, synthetic supramolecular assemblies share many similarities with biological assemblies, especially enzymes. The assemblies can be on the same length scale, and their structures and guest binding are typically governed by non-covalent interactions. Thus, only relatively weak interactions define the shape of a synthetic supramolecule or the secondary and tertiary structure of a protein, such that the resulting dynamism makes structure elucidation challenging. For biomolecules such as peptides, proteins, glycans and lipids this has often been tackled using ion mobility–mass spectrometry (IM-MS), whereby analyte ions are separated according to their gas-phase mobility and their mass-to-charge ratio. IM-MS is an established method in omics, separation sciences and small-molecule structural chemistry, but has only recently grown in popularity for the study of synthetic supramolecular assemblies in the gas phase. This Review describes IM-MS techniques and how they can help us understand the structures of molecular self-assemblies, host–guest complexes and metallosupramolecular complexes. Ion mobility–mass spectrometry (IM-MS) is a gas-phase method for structural characterization — a tool prevalent in biology but only recently finding applications in supramolecular chemistry. This Perspective describes how IM-MS techniques give us information about the structures of molecular self-assemblies, host–guest complexes and metallosupramolecular systems.

Ion mobility–mass spectrometry of supramolecular complexes and assemblies