StAmP-DB: a platform for structures of polymorphic amyloid fibril cores

Bioinformatics. 2022 Apr 28;38(9):2636-2638. doi: 10.1093/bioinformatics/btac126.


Summary: Amyloid polymorphism is emerging as a key property that is differentially linked to various conformational diseases, including major neurodegenerative disorders, but also as a feature that potentially relates to complex structural mechanisms mediating transmissibility barriers and selective vulnerability of amyloids. In response to the rapidly expanding number of amyloid fibril structures formed by full-length proteins, we here have developed StAmP-DB, a public database that supports the curation and cross-comparison of experimentally determined three-dimensional amyloid polymorph structures.

Availability and implementation: StAmP-DB is freely accessible for queries and downloads at

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid* / chemistry
  • Humans
  • Neurodegenerative Diseases*


  • Amyloid