In silico Characterization of Retinal S-antigen and Retinol Binding Protein-3: Target against Eales' Disease

Abstract

In current study two important proteins of Eales' disease, i.e. Retinal S-antigen (RSAG) (P10523) and Retinol binding protein-3 (RBP-3) (P10745), retrieved from Swiss prot database, are analysed and characterized through in silico tools. Characterization is carried out in terms of molecular weight, atomic composition, isoelectric point, extinction coefficient, aliphatic index and instability index. Primary structure analysis of target proteins showed that most of the amino acids are hydrophobic in nature which was evident due to the high content of non-polar residues. Thermal stability, which is a notification regarding the flexibility in the structure of protein, is higher here, i.e. 88.27 for RSAG and 100.31 of RBP-3 suggesting their stability in a wide range of temperature. Secondary structure analysis of RBP-3 and RSAG reveals that RBP-3 mostly have alpha helices while RSAG have mixed secondary structures, i.e. the alpha helices, extended strands and random coils which is suggestive about the high structural conservity of protein. This evolutionary conservity makes RSAG a better target against Eales' disorder. Determination of phosphorylation as well as signal peptide cleavage sites is another integral part of in silico characterization, as these determinations confirms about the functional aspect of protein.

Keywords

• Eales' disease
• Retinal S-antigen
• Retinol binding protein-3
• Computational analysis
• Inflammation
• Haemorrhage