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| Type |
Poster Presentation |
| Area |
생명화학 |
| Room No. |
포스터발표장 |
| Time |
4월 21일 (금요일) 13:00~14:30 |
| Code |
BIO.P-298 |
| Subject |
Investigation of Oligomerization Process of Alpha-synuclein |
| Authors |
배진의, 김준곤*
고려대학교 화학과, Korea
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| Abstract |
Many human diseases arise from protein misfolding, in which neurodegenerative diseases such as Parkinson's disease (PD) are related to fibrillar aggregates called amyloid fibrils. Alpha-synuclein aggregates to form insoluble fibrils in pathological conditions such as Parkinson's disease. Alpha-synuclein which is found mainly at the tips of nerve cells (neurones) in the brain is a primary structural component of Lewy body fibrils. Although the oligomerization and further fibrillation of alpha-synuclein are critical factors in PD, the aggregation mechanism of alpha-synuclein is not clearly revealed. To understand the detailed process and compositional change of monomers, oligomers, and fibrils during the process, we performed quantitative and qualitative analysis at the same time. In quantitative analysis, matrix-assisted laser desorption ionization (MALDI)-MS and triple quadrupole-MS were performed. To avoid dissosication of oligomers into monomer during ionization process, cross-linking agents were adopted. In qualitative analysis, the conformational characteristics of the oligomers were investigated using ion mobility-mass spectrometry (IM-MS). |
| E-mail |
ui53210@naver.com |
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119th General Meeting of the KCS