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129th General Meeting of Korean Chemical Society & Exposition Structural insights into distinct amyloid aggregation dynamics in water and heavy water

Submission Date :
2 / 28 / 2022 , 15 : 46 : 39
Abstract Number :
Presenting Type:
Poster Presentation Analytical Chemistry Oral Presentation
Presenting Area :
Analytical Chemistry
Authors :
MyungKook Son, Dongjoon Im, Dongvin Kwak, Da Gyeong Hyun, Sooyeon Chae, Gyusub Yoon, Chanju Won, Hugh I. Kim*
Department of Chemistry, Korea University, Korea
Assigned Code :
ANAL.P-358 Assigend Code Guideline
Presenting Time :
April 14 (THU) 11:00~13:00
Amyloidosis is a disease related with oligomer-fibrils formed by self-assembly due to misfolding of amyloid proteins. The self-assembly of amyloid protein is achieved through intermolecular hydrophobic interactions, forming the unbranched beta-sheet structured fibrils. The fibrillation process is not easy to study because it has various fibrillation mechanisms that are affected by various biological factors such as pH, metal ions, and temperature. Examples of such amyloid proteins include α-synuclein, tau protein, and amyloid-β associated with degenerative brain disease. These proteins are intrinsically disordered proteins (IDPs) which do not have a distinct structure, and are proteins with a secondary structure, a random coil. Insulin (INS) is related to a injection localized amyloidosis. Contrary to IDPs, INS is a protein with a distinct secondary to quaternary structure. D2O is generally used as a solvent instead of H2O to observe the protein. However, D2O has different physical properties from H2O due to the isotope effect, which may affect the physical properties of proteins. In the first chapter, we investigated the distinct amyloid fibrillation processes of structured protein, human INS, in H2O and D2O using various spectroscopic tools, including 2D-IR spectroscopy. The following chapter discuss the amyloid fibrillation process of intrinsically disordered proteins, α-synuclein and K18. By employing molecular dynamics simulation, an umbrella sampling method, stability of protofibrils in H2O and D2O can be calculated and compared. Overall, this research aims to understand the H-D isotope effect on protein structures and fibrillation kinetics.