Table 2 Enrichment in hydrophobicity for human T-cell autoimmune epitopes that contain aggregating peptides.

From: Autoimmune Responses to Soluble Aggregates of Amyloidogenic Proteins Involved in Neurodegenerative Diseases: Overlapping Aggregation Prone and Autoimmunogenic regions

Dataset Average Hydrophobicity
All amorphous β-aggregates forming hexapeptides 35.6 ± 13.2
All amyloid fibril forming hexapeptides 38.0 ± 12.9
All amyloid fibril forming peptides of all lengths 32.3 ± 11.2
All human T-cell autoimmune epitopes 28.4 ± 7.6
All human T-cell autoimmune epitopes that contain amorphous β-aggregating hexapeptides 31.3 ± 4.3
All human T-cell autoimmune epitopes that contain amyloid fibril forming hexapeptides 31.9 ± 4.0
All human T-cell autoimmune epitopes that contain amyloid fibril forming peptides of all lengths 30.5 ± 4.4
All HLA-DP binding epitopes 30.3 ± 8.9
All HLA-DQ binding epitopes 26.9 ± 7.3
HLA-DQ binding epitopes that contain amorphous β-aggregating hexapeptides 31.3 ± 3.8
HLA-DQ binding epitopes that contain amyloid fibril forming hexapeptides 32.4 ± 3.3
HLA-DQ binding epitopes that contain amyloid fibril forming peptides of all lengths 31.8 ± 3.1
All HLA-DR binding epitopes 28.5 ± 7.5
HLA-DR binding epitopes that contain amorphous β-aggregating hexapeptides 31.3 ± 5.3
HLA-DR binding epitopes that contain amyloid fibril forming hexapeptides 31.6 ± 4.5
HLA-DR binding epitopes that contain amyloid fibril forming peptides of all lengths 30.1  ±  4.7
  1. Average and standard deviation values of intrinsic hydrophobicity of peptide sequences in a given dataset of aggregating peptides and epitopes were computed as described in Methods.