• P-ISSN2233-4203
  • E-ISSN2093-8950
  • ESCI, SCOPUS, KCI

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

Oligomer Complexes of the (VQIVYK + NNQQNY) and (VQIVYK + LYQLEN) Mixing Solutions

Mass Spectrometry Letters / Mass Spectrometry Letters, (P)2233-4203; (E)2093-8950
2019, v.10 no.1, pp.32-37
https://doi.org/10.5478/MSL.2019.10.1.32
Jung Yeon-Ji (Department of Applied Chemistry, Kumoh National In)
Shin Min-Ji (Department of Applied Chemistry, Kumoh National Institute of Technology)
Kim Ho-Tae (Department of Applied Chemistry, Kumoh National Institute of Technology)
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Abstract

The π-π interactions of the peptide-dimer and peptide-trimer complexes were investigated in the (VQIVYK + LYQLEN) and (VQIVYK + NNQQNY) mixing solutions. The results showed that tyrosine (Y) residues were critical in the for-mation of hetero peptide-dimers and -trimers during the early oligomerization process. We used collision-induced dissociation (CID) along with electrospray ionization mass spectroscopy (ESI-MS) to obtain the structural information of the hetero-dimers and -trimers. We chose three amyloidogenic peptides–VQIVYK, NNQQNY, and LYQLEN–from tau protein, yeast prion-like protein Sup35, and insulin chain A, respectively. Hetero-dimer, -trimer, -tetramer, and -pentamer complexes were observed in the mass spectra. The tandem mass spectrum of the hetero-dimer and hetero-trimer showed two different fragmentation patterns (covalent and non-covalent bond dissociation). Y-Y interaction structures were also proposed for the hetero-dimer and -trimer complexes.

keywords
Peptide oligomer, VQIVYK, NNQQNY, LYQLEN, mass spectrometry (MS), MS/MS


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Submission Date
2018-12-17
Revised Date
2019-01-19
Accepted Date
2019-01-22
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