Hydrophilicity of Linear B-Epitopes

Abstract

Antigenic sites of a protein are those recognized by antibodies. Therefore it is most likely that these sites are accessible or on the surface of the protein, and these regions are probably more mobile than interior regions. Since these sites are on the surface, they are probably hydrophilic. Indeed, algorithms for hydrophilicity and accessibility have been used to predict antigenicity. In this research, the hydrophilicity by Parker’s scale, and hydrophobicityby Cornette, and Doolittle scales of linear b-rpitopes is studied on 344121 linear b-eptopes downloaded from iedb epitope database. Descriptive statistical analyses revealed that average hydrophilicity of these b-epitopes distributes normally with mean =2.1993, standard deviation σ=1.9303, skewness s= - 0.2681, and kurtosis =3.1826. It is seen that mean hydrophobicities are also distribute normally. A detailed review is performed to scan available hydrophophilicity/hydrophobicity scales. Altogether 24 scales are listed.