- P-ISSN 2233-4203
- E-ISSN 2093-8950
- P-ISSN2233-4203
- E-ISSN2093-8950
- ESCI, SCOPUS, KCI
Article Detail
Home > Article Detail
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
https://doi.org/10.5478/MSL.2021.12.4.179
(Kumoh National Institute of Technology)
(Kumoh National Institute of Technology)
(Kumoh National Institute of Technology)
Kim,
J., &
Kim,
H.
(2021). Fragmentation Analysis of rIAPP Monomer, Dimer, and [M rIAPP + M hIAPP ]5+ Using Collision-Induced Dissociation with Electrospray Ionization Mass Spectrometry. Mass Spectrometry Letters, 12(4), 179-185, https://doi.org/10.5478/MSL.2021.12.4.179
- Downloaded
- Viewed
Abstract
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.
- keywords
- rat islet amyloid polypeptide (rIAPP), human islet amyloid polypeptide (hIAPP), heterogeneous dimer, collision- induced dissociation mass spectrometry (CID-MS), MS/MS
- Submission Date
- 2021-10-28
- Revised Date
- 2021-11-12
- Accepted Date
- 2021-11-25
Other articles from this issue
- Special Issue in Honor of Prof. Seung Koo Shin
- Looking through the Mass-to-Charge Ratio: Past, Present and Future Perspectives
- Integrated Thermochemical Approach to Collision-Induced Dissociation Process of Peptides
- Ion Mobility Signatures of Glutamine-Containing Tryptic Peptides in the Gas Phase
- Elucidating H/D-Exchange Mechanism of Active Hydrogen in Aniline and Benzene-1,2-dithiol
- Li+ and Li+I−Li+ ions Solvated by 1,4-dioxane: An ion Mobility Spectrometry-Mass Spectrometry Study
- Effect of Cation Complexation of Hindered Phenol Antioxidants on their Fragmentation in Electrospray Ionization Tandem Mass Spectrometry
- LC-MS/MS-based Proteomic Analysis to Identify Protein Phosphorylation in Emiliania huxleyi
- Identification of HYIpro-3-1 Metabolites, a Novel Anti-Inflammatory Compound, in Human Liver Microsomes by Quadrupole-Orbitrap High-Resolution Mass Spectrometry
- Fragmentation Analysis of rIAPP Monomer, Dimer, and [M rIAPP + M hIAPP ]5+ Using Collision-Induced Dissociation with Electrospray Ionization Mass Spectrometry
- Separation of Light Rare-Earth Elements Using Gas-Pressurized Extraction Chromatography
- Molecular Characterization of Dissolved Organic Matter Unveils their Complexity, Origin, and Fate in Glacier and Glacial-Fed Streams and Lakes on the Tibetan Plateau
- Development of a Sensitive Analytical Method of Polynemoraline C Using LC-MS/MS and Its Application to a Pharmacokinetic Study in Mice
- more
Recommanded Articles
This website recommended the use the Chrome browser for journal website.