High-Throughput Fluorescence Profiling of Remodeling Dynamics at Surface-Deposited Amyloid Interfaces
Taeha Lee1,2, Yeongjun Seo1, Wonjun Hwang1
1Department of Biotechnology and Bioinformatics, Korea University, Sejong 30019, South Korea.
Analytical Chemistry
|June 16, 2026
Summary
A new 96-zone amyloid-deposited paper plate (96-ADPP) platform enables precise sensing of amyloid remodeling dynamics at interfaces. This high-throughput method reveals order-dependent effects of compound combinations on amyloid deposits.
Area of Science:
- Biochemistry
- Materials Science
- Analytical Chemistry
Background:
- Sensing amyloid remodeling at interfaces is difficult with conventional methods.
- Existing platforms struggle with spatially heterogeneous surface deposits.
Purpose of the Study:
- Develop a novel platform for quantitative sensing of amyloid remodeling at interfaces.
- Enable high-throughput analysis of amyloid-modulating agents and their combinations.
Main Methods:
- Introduced a 96-zone amyloid-deposited paper plate (96-ADPP) on a cellulose matrix.
- Utilized matched fluorescence quantification and spatial imaging across identical assay zones.
- Profiled remodeling responses to five amyloid-modulating agents and analyzed compound combinations.
Main Results:
- The 96-ADPP platform demonstrated reproducible interface-based sensing.
- Observed both signal amplification and reduction in response to modulating agents.
- Sequential treatment (puerarin then EPPS) showed superior amyloid signal reduction compared to combined administration.
Conclusions:
- The 96-ADPP is a high-throughput platform for profiling amyloid remodeling dynamics at interfaces.
- The platform facilitates systematic analysis of pairwise interactions and order-dependent responses.
- This method advances the study of amyloid-biointerface interactions and drug development.
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