The dept. of Biological Science Seminar: Molecular understanding of disease-causing protein aggregation
- 2019-05-14
The department of biological science will hold the following seminar.
Title: Molecular understanding of disease-causing protein aggregation
Speaker: Dr. Lee Young-ho (Korea Basic Science Institute, KBSI)
Date & Time: May. 16. (Thu.) 2019 5:00 PM
Place: Basic Science Institute Seminar Room (Natural Science 1) No. 31317
Abstract: Nascent proteins fold into native structures in soluble states for gain of function. Failure of keeping native structures and eliminating misfolded/aggregated proteins often induces protein aggregation with loss of function and gain of disease such as Alzheimer's disease (AD), Parkinson's disease (PD), and type 2 diabetes mellitus (T2DM).1,2 Despite of countless efforts, much remains to be elucidated on underlying principles of protein misfolding and aggregation from the microscopic and macroscopic point of view. In my talk, I will first show microscopic molecular mechanisms of protein aggregation, amyloid fibrillation and amorphous aggregation, with the general description on the structures of amyloidogenic precursors and amyloid fibrils.3-5 Aggregation of several amyloidogenic proteins and peptides such as Alzheimer`s amyloid b peptides in AD, a-synuclein in PD, and insulin in T2DM will be explained based mostly on our previous and on-going studies. Macroscopic viewpoints including solubility, supersaturation, and phase diagram for amyloid formation will be next given.6-9 Several case studies which aimed at inhibiting toxic amyloid aggregation will be lastly addressed.10
References: [1] Lee Y.-H. et. al., Biochim. Biophys. Acta.- Proteins Proteom. (2019); [2] Terakawa M.S., et. al. Biochim. Biophys. Acta.-Biomembr. (2018); [3] Lee Y.-H. and Ramamoorthy A, Protein Sci. (2018); [4] Terakawa M.S. and Lee Y.-H. et. al., Biochim. Biophys. Acta.-Biomembr. (2018); [5] Kinoshita M. et. al., Phys. Chem. Chem. Phys. (2017); [6] Terakawa M.S. et. al., J. Biol. Chem. (2014); [7] Korshavn K.J. et. al., J. Biol. Chem. (2017); [8] Lin Y. et. al., Langmuir (2016); [9] Ikenoue T.* and Lee Y.-H.* et. al., Angewandte chemie (2014); [10] Ikenoue T.* and Lee Y.-H.* et. al., Proc. Natl. Acad. Sci. USA. (2014); [11] Kim D. et. al, Nature Nanotechnol., (2018)