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.

Documentation

Links