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  • 09월 03일 23시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

대한화학회 제122회 학술발표회 및 총회 Inhibition mechanism of human serum albumin in alpha-synuclein aggregation

등록일
2018년 8월 22일 12시 23분 01초
접수번호
0876
발표코드
ANAL.P-354 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
10월 19일 (금요일) 11:00~12:30
발표형식
포스터
발표분야
Analytical Chemistry
저자 및
공동저자
Tae Su Choi, Hugh I. Kim*
Department of Chemistry, Korea University, Korea
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.

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