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  • 02월 20일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제113회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Understanding the Role of Denaturation and Hydrophobic Interaction in Amyloid Fibrillation of Insulin

2014년 2월 18일 13시 59분 39초
PHYS.O-8 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
금 11시 : 40분
물리화학 - General Oral Presentation
저자 및
최태수, 김준곤*
포항공과대학교 화학과, Korea
Amyloid fibrillation is an abnormal aggregation phenomenon of amyloidogenic proteins, which are highly correlated with senile disorders such as Alzheimer’s disease, Parkinson’s disease, type 2 diabetes, and spongiform encephalopathy. The fibrillation process of amyloidogenic proteins is initiated by exposing hydrophobic residues to solvent molecules (denaturation of protein), and amyloid self-assembly occurs between hydrophobic residues of proteins (hydrophobic interaction). In the present study, we investigate the role of protein-solvent interaction to understand a correlation between denaturation and hydrophobic interaction during the fibrillation process of insulin. Thioflavin T assay and transmission electron microscopy (TEM) images exhibit that binary mixtures of water and formamide derivatives promotes the formation of insulin fibril compared with water. However, non-aqueous solutions of formamide derivatives suppress the formation of insulin fibril with much longer lag time than the presence of water. Solution small-angle X-ray scattering (SAXS) combined with molecular dynamics (MD) simulation suggests that fibrillation kinetics of insulin in the binary mixtures is highly promoted by the denaturation of B11-B17 core sequence residues. Differential scanning calorimetry (DSC) shows that the presence of water is crucial for intermolecular protein-protein hydrophobic interaction. These results indicate that both denaturation and hydrophobic interaction plays an important role in the amyloid fibrillation.