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  • 02월 28일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제123회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Charge effect of ATP on changing self-assembly mechanism of amyloidogenic proteins

2019년 2월 7일 15시 54분 05초
ANAL1.O-8 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
목 09시 : 28분
Analytical Chemistry - Oral Presentation of Young Analytical Chemists I
저자 및
Chae Eun Heo, Jong Yoon Han, Sooyeon Chae, Chae Ri Park, MyungKook Son, Min Ji Kim, Dongjoon Im, Paul Valery Migisha Ntwali , Gyeongseo Min, Chaehyeon Yoon, Hugh I. Kim*
Department of Chemistry, Korea University, Korea
Amyloid fibrillation is a biological process by which amyloid disease-related protein molecules are self-assembled by hydrophobic interactions. In human body, such amyloidogenic proteins (e.g. amyloid-β, α-synuclein, human islet amylin polypeptide, tau, lysozyme and insulin) exist with specific charge state, positive or negative, depending on their inherent isoelectric point. To build a well-aligned fibril by assembling same charged proteins, it must overcome the electrostatic repulsion between the same charged residues. Thus, numerous research has been reported that charged species abundant in our body (e.g. metal ion, DNA, nucleic acid, heparin, glycosaminoglycans etc.) influence to the mechanism of amyloid fibrillation by electrostatic interaction. Here, we have studied to understand the molecular mechanism of protein fibrillation under ATP, which is a small biological polyanion and is present in high levels in cell. Firstly, we have conducted the thioflavin T(ThT) assay which monitors the formation of amyloid fibril. To identify and characterize the protein complexes between protein and small molecules, we have utilized electrospray ionization mass spectrometry (ESI-MS) and ion mobility spectrometry (IMS), along with circular dichroism (CD) and solution small-angle x-ray scattering (SAXS). The experimental evidence obtained from these diverse analytical techniques, and subsequent studies about biological anion-mediated protein aggregation would be highly helpful in understanding the mechanistic details of amyloid fibrillation under the influence of external factors, which affect protein-protein interactions.