Oligomer Complexes of the (VQIVYK
- Authors
- Jung, Yeon-Ji; Shin, Min-Ji; Kim, 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.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - Department of Applied Chemistry > 1. Journal Articles
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.