Table 1.
Representative studies done by mass spectrometry (MS)-based techniques for early-stage oligomer analysis.
| Protein/peptide |
MS-based techniques |
Achievements | References |
|---|---|---|---|
| Aβ1−42 | Native top-down | Interaction between Aβ1−42 and metal ion | Lermyte et al., 2019 |
| NNQQNY VEALYL SSTNVG |
ESI-IM-MS | Mechanism of peptide assembly | Bleiholder et al., 2011 |
| hIAPP Aβ1−40 |
ESI-IM-MS | Mechanisms and binding patterns of small molecule inhibitors | Young et al., 2015; Hoffmann et al., 2017 |
| PrP | HDX-MS | Amyloid fibril formation mechanism | Singh and Udgaonkar, 2013 |
| β2m | HDX-MS | Mechanism of Cu(II) induced amyloid formation | Borotto et al., 2017 |
| Aβ1−42 | FPOP-MS | Conformational change of the aggregation process | Li et al., 2016 |
| Sup 35 | CX-MS | Mechanism of different folding patterns | Wong and King, 2015 |
| α-crystallin | CX-MS | Mechanism of αA66-80 peptide induced aggregation | Kannan et al., 2013 |
A1−42: Amyloid β1−42; hIAPP: human islet amyloid polypeptide; Aβ1−40: Amyloid β1−40; PrP: prion protein; β2m: β2-microglobulin; ESI: electrospray ionization; IM: ion mobility; HDX: hydrogen/deuterium exchange; FPOP: fast photochemical oxidation of proteins; CX: Chemical cross-linking.