Abstract: To further understand the structure-function relationship of the allergen Cra c 8 of triosephosphate isomerase (TPI) from brown shrimps (Crangon crangon) and the molecular basis of cross reaction among food allergens, physical and chemical properties as well as the difference and similarity between Cra c 8 and other triosephosphate isomerases at molecular level were analyzed by a series of bioinformatics softwares. The results showed that Cra c 8 protein was an acidic protein composed of 249 amino acids. The homology of similar proteins was relatively high and hydrophobic and hydrophilic areas had great similarity in Archaeopotamobius sibiriensis, Fenneropenaeus chinensis, Salmo salar, Triticum aestivum and Blattella germanica. The prediction results of secondary structure showed that α-helix and irregular folds were the major structures of Cra c 8 protein, while β-sheet and β-corner regions were absent. The spatial structure of Cra c 8 protein was successfully built by homology modeling. This study will provide a theoretical reference for exploring the activity and cross-reactivity properties of brown shrimp Cra c 8 protein.

Key words: bioinformatics, triosephosphate isomerase, allergen, homology modeling