|
|
| Type |
Poster Presentation |
| Area |
Analytical Chemistry |
| Room No. |
Grand Ballroom |
| Time |
10월 19일 (금요일) 11:00~12:30 |
| Code |
ANAL.P-354 |
| Subject |
Inhibition mechanism of human serum albumin in alpha-synuclein aggregation |
| Authors |
Tae Su Choi, Hugh I. Kim*
Department of Chemistry, Korea University, Korea
|
| Abstract |
Alpha-synuclein, one of amyloid proteins that are related to the pathology of alpha-synucleinopathies (e.g. Parkinson's disease, dementia with Lewy bodies, and multiple system atrophies), self-assembles to fibrillar aggregates toxic to neuronal cells. Interestingly, the formation of alpha-synuclein aggregates is not common in human organs except for brains. As one of hypothesis, molecular interaction with plasma proteins in human fluids has been suggested to disrupt protein-protein interactions of alpha-synuclein. Human serum albumin is the most abundant protein in human fluid and is known to suppress the self-assembly of amyloid-beta peptide. Thus, human serum albumin is expected to modulate the self-assembly of alpha-synuclein. In this poster presentation, I will discuss the molecular interaction between alpha-synuclein and human serum albumin. Using multiple biophysical approaches, I have characterized that electrostatic interaction of alpha-synuclein and human serum albumin plays a crucial role in suppressing the aggregation of alpha-synuclein. |
| E-mail |
choitaesu@korea.ac.kr |
|
122nd General Meeting of the KCS