abs

학술발표회초록보기

Inquiry on Abstract abstract@kcsnet.or.kr

Inquiry on Payment member@kcsnet.or.kr

현재 가능한 작업은 아래와 같습니다.
  • 03월 02일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

129th General Meeting of Korean Chemical Society & Exposition Purification of Non-Tagged Recombinant α-Synuclein Using Liquid Chromatography Based Separation Methods

Submission Date :
2 / 22 / 2022 , 18 : 43 : 12
Abstract Number :
129022230387
Presenting Type:
Oral Presentation
Presenting Area :
Analytical Chemistry - Oral Presentation of Young Analytical Chemists II
Authors :
Da Gyeong Hyun, Dongjoon Im, MyungKook Son, Sooyeon Chae, Dongvin Kwak, Chanju Won, Gyusub Yoon, Hugh I. Kim*
Department of Chemistry, Korea University, Korea
Assigned Code :
ANAL2.O-18 Assigend Code Guideline
Presenting Time :
FRI, 10 : 08
α-Synuclein aggregates are the pathological hallmarks of synucleinopathies, including Parkinson’s disease and dementia with Lewy bodies. However, there is still no treatment for the synucleinopathies that has been established. To develop a therapeutic strategy, it is crucial to understand the molecular basis of α-synuclein aggregation and suppress the pathogenic amyloid aggregate formation. Up to date, as in-human studies are limited, the majority of research findings were based on in vitro experiments, with purified recombinant α-synuclein used to investigate self-assembly properties. Herein, we developed high-purity recombinant full-length α-synuclein expression and purification protocols without affinity tags or linkers. Furthermore, we performed a quality assessment of purified recombinant proteins to confirm the unique properties of α-synuclein via biophysical analyses including mass spectrometry-based identification, thioflavin T (ThT) fluorescence assay, and circular dichroism (CD). The compelling results imply that the proposed non-tagged α-synuclein preserves its biophysical properties, which can be used in further study to investigate the self-assembly property of α-synuclein.