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Updated: Oct 2, 2025
09:00
Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain
Published on: April 28, 2022
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StAmP-DB: a platform for structures of polymorphic amyloid fibril cores
Nikolaos Louros1,2, Rob van der Kant1,2, Joost Schymkowitz1,2
1Switch Laboratory, VIB-KU Leuven Center for Brain & Disease Research, 3000 Leuven, Belgium.
Bioinformatics (Oxford, England)
|February 24, 2022
Summary
Amyloid polymorphism, linked to neurodegenerative diseases and transmissibility, is explored through StAmP-DB. This database curates and compares 3D amyloid structures, aiding research into these complex diseases.
Area of Science:
- Biochemistry
- Structural Biology
- Neuroscience
Background:
- Amyloid polymorphism is crucial in conformational diseases like neurodegenerative disorders.
- Amyloid structures influence transmissibility and vulnerability.
Purpose of the Study:
- To develop a public database for amyloid polymorph structures.
- To support curation and cross-comparison of experimentally determined 3D amyloid structures.
Main Methods:
- Development of StAmP-DB, a public database.
- Curation of experimentally determined 3D amyloid polymorph structures.
Main Results:
- StAmP-DB provides a centralized resource for amyloid structure data.
- Facilitates comparative analysis of diverse amyloid polymorphs.
Conclusions:
- StAmP-DB aids in understanding amyloid polymorphism's role in disease.
- The database supports research on neurodegenerative disorders and amyloid structures.
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