Presentation Information

10:45 AM - 11:00 AM JST(1:45 AM - 2:00 AM UTC)

[23a-1BN-7]Difference in LSPR sensitivity for detection of α-synuclein amyloid protein depending on the nanostructure geometry

〇Yuto Kimura¹, Takumi Kinoshita¹, Carl Frederik Werner¹, Noriyuki Hasuike¹, Masayuki Fukuzawa², Minoru Noda¹, Toshinori Shimanouch³ (1.Electronics,Kyoto inst. tech., 2.Information science,Kyoto inst. tech., 3.Life Science, Okayama Univ)

Keywords:

LSPR,alpha synuclein,Parkinson's disease

We have previously developed and confirmed a localized surface plasmon resonance (LSPR) sensor to detect αSyn aggregates for the very early diagnosis of Parkinson's disease (PD). In this study, we verified the difference in αSyn aggregates detectability between two lipids (DPPC and DMPC) and their structures (monolayer and bilayer). As a result, the largest peak shift (8.1 nm/70 nM) was observed when the DMPC bilayer was immobilized. The interactions between αSyn and those different lipids and their structures were also evaluated by QCM to confirm the above results.

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