title: Fcγ1 fragment of IgG1 as a powerful affinity tag in recombinant Fc-fusion proteins: immunological, biochemical and therapeutic properties.
abstract: Affinity tags are vital tools for the production of high-throughput recombinant proteins. Several affinity tags, such as the hexahistidine tag, maltose-binding protein, streptavidin-binding peptide tag, calmodulin-binding peptide, c-Myc tag, glutathione S-transferase and FLAG tag, have been introduced for recombinant protein production. The fragment crystallizable (Fc) domain of the IgG1 antibody is one of the useful affinity tags that can facilitate detection, purification and localization of proteins and can improve the immunogenicity, modulatory effects, physicochemical and pharmaceutical properties of proteins. Fcγ recombinant forms a group of recombinant proteins called Fc-fusion proteins (FFPs). FFPs are widely used in drug discovery, drug delivery, vaccine design and experimental research on receptor-ligand interactions. These fusion proteins have become successful alternatives to monoclonal antibodies for drug developments. In this review, the physicochemical, biochemical, immunological, pharmaceutical and therapeutic properties of recombinant FFPs were discussed as a new generation of bioengineering strategies.
authors.affiliation: a Microbiology & Virology Research Center, Bu-Ali Research Institute, Mashhad University of Medical Sciences , Mashhad, Iran.
authors.forename: Saman
authors.initials: S
authors.lastname: Soleimanpour
authors.affiliation: b Internal medicine Department, Arash Hospital, the College of Medicine, Tehran University of Medical Sciences , Tehran, Iran.
authors.forename: Tahereh
authors.initials: T
authors.lastname: Hassannia
authors.affiliation: c Inflammation and Inflammatory Diseases Research Center, Medical School, Mashhad University of Medical Sciences , Mashhad, Iran.
authors.forename: Mahdieh
authors.initials: M
authors.lastname: Motiee
authors.affiliation: d Department of Immunology, faculty of medicine, Kurdistan University of Medical Sciences , Sanandaj, Iran.
authors.forename: Abbas Ali
authors.initials: AA
authors.lastname: Amini
authors.affiliation: c Inflammation and Inflammatory Diseases Research Center, Medical School, Mashhad University of Medical Sciences , Mashhad, Iran.
authors.forename: S A R
authors.initials: SA
authors.lastname: Rezaee
mesh_terms: D000345:Affinity Labels / Q000737:chemistry; D000818:Animals; D001665:Binding Sites; D006801:Humans; D007141:Immunoglobulin Fc Fragments / Q000737:chemistry / Q000276:immunology* / Q000627:therapeutic use*; D007074:Immunoglobulin G / Q000737:chemistry / Q000276:immunology* / Q000627:therapeutic use*; D015202:Protein Engineering / Q000379:methods; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000276:immunology* / Q000627:therapeutic use*
chemical_list: D000345:Affinity Labels; D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D011993:Recombinant Fusion Proteins
keywords: Affinity tag; Fc-fusion; Fcγ; recombinant protein; stability