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Oligomer Complexes of the (VQIVYK

Authors
Jung, Yeon-JiShin, Min-JiKim, Ho-Tae
Issue Date
Mar-2019
Publisher
KOREAN SOC MASS SPECTROMETRY
Keywords
Peptide oligomer; VQIVYK; NNQQNY; LYQLEN; mass spectrometry (MS); MS/MS
Citation
MASS SPECTROMETRY LETTERS, v.10, no.1, pp 32 - 37
Pages
6
Journal Title
MASS SPECTROMETRY LETTERS
Volume
10
Number
1
Start Page
32
End Page
37
URI
https://scholarworks.bwise.kr/kumoh/handle/2020.sw.kumoh/25551
DOI
10.5478/MSL.2019.10.1.32
ISSN
2233-4203
2093-8950
Abstract
The pi-pi 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 formation 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.
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