AmyloGraph: a comprehensive database of amyloid-amyloid interactions.

Area of Science:

• Biochemistry
• Structural Biology
• Biophysics

Background:

• Information on amyloid protein interactions affecting fibrillization is fragmented across numerous publications.
• Existing data lacks a standardized format, hindering systematic analysis and research.
• Amyloid proteins are implicated in various neurodegenerative diseases, making their interactions crucial to study.

Purpose of the Study:

• To curate and consolidate experimentally determined amyloid-amyloid interactions into a structured database.
• To develop and implement a novel, standardized terminology for describing these interactions.
• To provide a publicly accessible resource for researchers studying amyloid aggregation and cross-talk.

Main Methods:

• Manual curation of data from approximately 200 scientific publications (selected from 562 initial sources).
• Extraction of details on 883 experimentally verified interactions involving 46 different amyloid proteins or peptides.
• Development of a standardized nomenclature for amyloid-amyloid interactions, including inhibition and cross-seeding phenomena.

Main Results:

• Compilation of 883 unique amyloid-amyloid interactions, representing a significant expansion of accessible data.
• Introduction of a novel, standardized terminology for describing various types of amyloid cross-talk.
• Establishment of AmyloGraph, the sole publicly available repository for experimentally determined amyloid-amyloid interactions.

Conclusions:

• AmyloGraph provides a well-defined and comprehensive dataset for studying amyloid protein interactions.
• The standardized terminology facilitates more precise and reproducible research in the field of amyloidogenesis.
• The online database and R package offer accessible tools for the scientific community to explore amyloid interactions.