Determination of Physicochemical Properties of Human Immunoglobulin G- Fc Fragment by Bioinformatic

Abstract

Introduction: Immunoglobulins (Igs) are defensive glycoproteins specifically recognize and destroy pathogens. Immunoglobulin G (IgG) is most abundant Ig in serum has important protective role against infections. Fragment of crystallizable (Fc) in IgG has essential role in pathogens destruction. Determination the physicochemical properties of IgG Fc is useful in well recognition of its function, diagnostic and therapeutic purposes. Bioinformatic is an efficient scientific field uses abundant biological information collected in computers for solving biologic problems. Aim of this study is recognition the physicochemical features of human IgGFc by bioinformatic. Materials and Methods: Amino acid sequence and third structure of reference human IgG were found in PDB (Protein Data Bank) database. Second IgG structure was determined by Protein Homology/analogY Recognition Engine V 2 (Phyre 2) software. Physicochemical properties (felexibility, accessibility and hydrophilicity) of IgGFc fragment were identified by IEDB (Immune Epitope Database) software. Results: According to results of this study, most accessibe, hydrophilic and felexible sites of IgGFc fragment were located to 200 – 450 amino acid sequences. Moreover most accessibe, hydrophilic and felexible positions were overlapped in 291300 and 381400 amino acid sequences and could be most probable locations of epitopes. Conclusion: Physicochemical properties of IgGFc fragment identified in present study are valuable in more exact recognition of IgG functions and its immunogenic epitopes which could be helpful in producing of specific monoclonal anti IgG antibodies for production IgG diagnostic tools, optimizing existing kits, development of similar proteins for diagnostic and therapeutic purposes and phylogenic studies.