AMYLPRED
AMYLPRED predicts amyloidogenic regions in proteins from primary amino-acid sequence to provide consensus-based identification of aggregation-prone stretches relevant to amyloid fibril formation.
Key Features:
- Consensus prediction: Integrates five independently published sequence-based prediction algorithms to produce a consensus identification of amyloidogenic regions.
- Primary structure input: Operates solely on protein primary (amino-acid) sequence data for sequence-based prediction.
- Identification of novel determinants: Flags previously unreported peptide stretches predicted to be amyloidogenic for experimental follow-up.
- Surface localization assessment: Predictions and experimentally validated determinants have been analyzed for surface exposure using DSSP and molecular graphics programs.
Scientific Applications:
- Protein misfolding research: Maps aggregation-prone regions to support studies of amyloidoses and amyloid fibril formation mechanisms.
- Experimental prioritization: Prioritizes candidate peptide stretches for biochemical and biophysical validation of amyloidogenicity.
- Therapeutic target identification: Guides identification of sequence regions that may serve as targets for strategies to inhibit amyloid formation.
Methodology:
AMYLPRED applies five distinct published sequence-based prediction algorithms in tandem to generate a consensus from the primary amino-acid sequence; predictions have been corroborated using molecular graphics programs O and PyMOL and the DSSP algorithm.
Topics
Collections
Details
- Tool Type:
- web application
- Operating Systems:
- Linux, Windows, Mac
- Programming Languages:
- Python
- Added:
- 8/3/2017
- Last Updated:
- 11/25/2024
Operations
Publications
Frousios KK, Iconomidou VA, Karletidi C, Hamodrakas SJ. Amyloidogenic determinants are usually not buried. BMC Structural Biology. 2009;9(1). doi:10.1186/1472-6807-9-44. PMID:19589171. PMCID:PMC2714319.