초록문의 abstract@kcsnet.or.kr

결제문의 member@kcsnet.or.kr

현재 가능한 작업은 아래와 같습니다.
  • 02월 28일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제123회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Histidine (δδδ) and (εεε) tautomer effect on early oligomerization stage of the amyloid-beta peptide (1-40)

2019년 2월 14일 15시 17분 17초
PHYS.P-208 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
4월 19일 (금요일) 11:00~12:30
Physical Chemistry
저자 및
Salimi Abbas, Hao Li1, Sompriya Chatterjee1, Jin yong Lee2,*
Sungkyunkwan University, Iran
1department of Chemistry, Sungkyunkwan University, Korea
2Department of Chemistry, Sungkyunkwan University, Korea
As one of the main types of dementia, the Alzheimer disease (AD) is connected to the accumulation of amyloid-beta peptide (Aβ) in the brain. Important factors such as amyloid concentration, pH, solvent, histidine behavior and metal ions can affect the aggregation progress. Aβ oligomer hypothesis and experimental results have shown the higher toxicity of small oligomers (dimers, trimers, etc.) compare with fibrils which indicates the importance of investigation of aggregation at the early stages in details. Since many aspects at this level is still unknown so here molecular dynamic (MD) simulation of Aβ(1-40) homodimers considering the (δδδ) and (εεε) tautomeric effects with different initial conformations were performed using GROMACS 5.0 software to elucidate structure changes during aggregation. Results showed very low propensity or almost no tendency to form β-sheet for (εεε) homodimers. However in (δδδ) homodimers higher content of β-sheet during aggregation can be observed which may show the higher neurotoxicity. Also β-sheet formation in (δδδ) dimers can be found in almost same regions (CHC and C-/N- terminal). Our study may provide better understanding of tautomeric behavior of histidine on Aβ(1-40) aggregation and disease progression which may lead to find some ways to cure the AD.