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  • P-ISSN 2233-4203
  • E-ISSN 2093-8950

Fragmentation Analysis of rIAPP Monomer, Dimer, and [M rIAPP + M hIAPP ]5+ Using Collision-Induced Dissociation with Electrospray Ionization Mass Spectrometry

Mass Spectrometry Letters / Mass Spectrometry Letters, (P)2233-4203; (E)2093-8950
2021, v.12 no.4, pp.179-185
Kim Jeongmo (Kumoh National Institute of Technology)
Kim Ho-Tae (Kumoh National Institute of Technology)
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Collision-induced dissociation (CID) combined with electrospray ionization mass spectrometry (ESI-MS) was used to obtain structural information on rat islet amyloid polypeptide (rIAPP) monomers (M) and dimers (D) observed in the multiply charged state in the MS spectrum. MS/MS analysis indicated that the rIAPP monomers adopt distinct structures depending on the molecular ion charge state. Peptide bond dissociation between L 27 and P 28 was observed in the MS/MS spectra of rIAPP monomers, regardless of the monomer molecular ion charge state. MS/MS analysis of the dimers indicated that D 5+ comprised M 2+ and M 3+ subunits, and that the peptide bond dissociation process between the L 27 and P 28 residues of the monomer subunit was also maintained. The observation of (M+ b 27 ) 4+ and (M+ y 10 ) 3+ fragment ions were deduced to originate from the two differ-ent D 5+ complex geometries, the N-terminal and C-terminal interaction geometries, respectively. The fragmentation pattern of the [M rIAPP + M hIAPP ] 5+ MS/MS spectrum showed that the interaction occurred between the two N-terminal regions of M rIAPP and M hIAPP in the heterogeneous dimer (hetero-dimer) D 5+ structure.

rat islet amyloid polypeptide (rIAPP), human islet amyloid polypeptide (hIAPP), heterogeneous dimer, collision- induced dissociation mass spectrometry (CID-MS), MS/MS

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