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제126회 대한화학회 학술발표회 및 총회 Comparison of Fibrillation Kinetics of Amyloid Proteins in H2O and D2O

2020년 9월 10일 14시 53분 31초
ANAL1.O-14 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
화 09시 : 52분
Analytical Chemistry - Oral Presentation of Young Analytical Chemists I
저자 및
MyungKook Son, Chae Ri Park, Chae Eun Heo, Dongjoon Im, Min Ji Kim, Sooyeon Chae, Hugh I. Kim*
Department of Chemistry, Korea University, Korea
Heavy water, D2O, has been used in Infra-Red (IR) spectroscopy, Nuclear Magnetic Resonance (NMR), etc., to avoid the interference of O-H frequencies and H resonance frequency when light water, H2O is used. Specifically for IR, amide I band of peptides and proteins is 1600-1700 cm-1, while the H2O vibrational frequency is 1643.5 cm-1 overlapping the amide I band. Also, hydrogen-deuterium exchange (HDX) mass spectrometry is utilized to study protein tertiary structures. But since D2O is more polar than that of H2O, the hydrophobic effect of D2O is also stronger. So, the properties of the protein in H2O and D2O for example, protein stability, can be different. Efimova et al., have compared the stability of globular protein, lysozyme and bovine serum albumin in H2O and D2O, using differential scanning calorimetry (DSC). Proteins were more stable in D2O, with a wider pH range of stable form of BSA. There are some similar studies, but little about the protein fibrillation in D2O is known. Hydrophobic interaction of proteins is significant to the fibrillation of amyloidogenic proteins and protein structures. In this study, we have compared the hydrophobic interactions, structures and stability of amyloidogenic proteins, insulin and alpha-synuclein, using various spectroscopic methods, Fourier transform IR (FT-IR) spectroscopy, 2D-IR spectroscopy, ion mobility mass spectrometry, small angle x-ray scattering, thioflavin-T assay, DSC, etc.