Interferon dimers: IFN-PEG-IFN

References

• Cordes AA, Platt CW, Carpenter JF, et al. Selective domain stabilization as a strategy to reduce fusion protein aggregation. J Pharm Sci. 2012;101:1400–1409.
   PubMed Web of Science ®Google Scholar
• Chang C-H, Gupta P, Goldenberg DM. Advances and challenges in developing cytokine fusion proteins as improved therapeutics. Expert Opin Drug Discov. 2009;4:181–194.
   PubMed Web of Science ®Google Scholar
• Marianayagam N, Sunde M, Matthews J. The power of two: protein dimerization in biology. Trends Biochem Sci. 2004;29:618–625.
   PubMed Web of Science ®Google Scholar
• Isaacs A, Lindenmann J. Virus interference. I. The interferon. Proc R Soc B Biol Sci. 1957;147:258–267.
   PubMed Web of Science ®Google Scholar
• Brassard D, Grace M, Bordens R. Interferon-alpha as an immunotherapeutic protein. J Leukoc Biol. 2002;71:565–581.
   PubMed Web of Science ®Google Scholar
• Bell SJ, Fam CM, Chlipala EA, et al. Enhanced circulating half-life and antitumor activity of a site-specific pegylated interferon-alpha protein therapeutic. Bioconjug Chem. 2008;19:299–305.
   PubMed Web of Science ®Google Scholar
• Nagabhushan T, Reichert P, Walter M, et al. Type I interferon structures: possible scaffolds for the interferon-alpha receptor complex. Can J Chem. 2002;80:1166–1173.
   Web of Science ®Google Scholar
• Radhakrishnan R, Walter L, Hruza A, et al. Zinc mediated dimer of human interferon-alpha 2b revealed by X-ray crystallography. Structure. 1996;4:1453–1463.
   PubMed Web of Science ®Google Scholar
• Nisonoff A, Rivers MM. Recombination of a mixture of univalent antibody fragments of different specificity. Arch Biochem Biophys. 1961;63:460–462.
   Web of Science ®Google Scholar
• Brennen M. Preparation of bispecific antibodies by chemical recombinant of monoclonal immunoglobulin G1 fragments. Science. 1985;229:81–83.
   PubMed Web of Science ®Google Scholar
• Doppalapudi VR, Huang J, Liu D, et al. Chemical generation of bispecific antibodies. Proc Natl Acad Sci USA. 2010;107:22611–22616.
   PubMed Web of Science ®Google Scholar
• Xiao J, Hamilton B, Tolbert T. Synthetic of N-terminally linked protein and peptide dimers by native chemical ligation. Bioconjug Chem. 2010;21:1943–1947.
   PubMed Web of Science ®Google Scholar
• Pasche N, Neri D. Immunocytokines: a novel class of potent armed antibodies. Drug Discov Today. 2012;17:583–590.
   PubMed Web of Science ®Google Scholar
• Kontemann R. Dual targeting strategies with bispecific antibodies. MAbs. 2012;4:182–197.
   PubMed Web of Science ®Google Scholar
• Fischer N, L Eacute Ger O. Bispecific antibodies: molecules that enable novel therapeutic strategies. Pathobiology. 2007;74:3–14.
   PubMed Web of Science ®Google Scholar
• Schellinger J, Kudupudi A, Natarajan A, et al. A general chemical synthesis platform for crosslinking multivalent single chain variable fragments. Org Biomol Chem. 2012;10:1521–1526.
   PubMed Web of Science ®Google Scholar
• Liu R, Ji D, Wang J, et al. Preparation, characterization and in vitro bioactivity of N-terminally PEGylated staphylokinase dimers. Process Biochem. 2012;47:41–46.
   Web of Science ®Google Scholar
• Mack ET, Snyder PW, Perez-Castillejos R, et al. Using covalent dimers of human carbonic anhydrase II to model bivalency in immunoglobulins. J Am Chem Soc. 2011;133:11701–11715.
   PubMed Web of Science ®Google Scholar
• Lorenzo M, Decker C, Kahveci M, et al. Homodimeric Protein-Polymer Conjugates via the Tetrazine-trans-Cyclooctene Ligation. Macromolecules. 2015;49:30–37.
   PubMed Web of Science ®Google Scholar
• Mammen M, Choi S, Whitesides GM. Polyvalent interactions in biological systems: implications for design and use of multivalent ligands and inhibitors. Angew Chem Int Ed. 1998;37:2754–2794.
   PubMed Web of Science ®Google Scholar
• Dalle B, Henri A, Rouyer-Fessard P, et al. Dimeric erythropoietin fusion protein with enhanced erythropoietic activity in vitro and in vivo. Blood. 2001;97:3776–3782.
   PubMed Web of Science ®Google Scholar
• Chang C, Rossi E, Cardillo T, et al. A new method to produce mono-PEGylated dimeric cytokines shown with human interferon-alpha-2b. Bioconjug Chem. 2009;20:1899–1907.
   PubMed Web of Science ®Google Scholar
• Fidler K, Jevševar S, Milunovic T, et al. The characterisation and potential use of G-CSF dimers and their PEGylated conjugates. Acta Chim Slov. 2011;58:1–8.
   PubMed Web of Science ®Google Scholar
• Balan S, Choi JW, Godwin A, et al. Site-specific PEGylation of protein disulfide bonds using a three-carbon bridge. Bioconjug Chem. 2007;18:61–76.
   PubMed Web of Science ®Google Scholar
• Brocchini S, Balan S, Godwin A, et al. PEGylation of native disulfide bonds in proteins. Nat Protoc. 2006;1:2241–2252.
   PubMed Web of Science ®Google Scholar
• Khalili H, Khaw P, Lever R, et al. Fab-PEG-Fab as a potential antibody mimetic. Bioconjug Chem. 2013;24:1870–1882.
   PubMed Web of Science ®Google Scholar
• Khalili H, Lee R, Khaw P, et al. An anti-TNF alpha antibody mimetic to treat ocular inflammation. Sci Rep. 2016;6:36905.
   PubMed Web of Science ®Google Scholar
• Vauquelin G, Charlton SJ. Exploring avidity: understanding the potential gains in functional affinity and target residence time of bivalent and heterobivalent ligands. Br J Pharmacol. 2013;168:1771–1785.
   PubMed Web of Science ®Google Scholar
• Vauquelin G, Charlton SJ. Long-lasting target binding and rebinding as mechanisms to prolong in vivo drug action. Br J Pharmacol. 2010;161:488–508.
   PubMed Web of Science ®Google Scholar
• Khalili H, Khaw P, Brocchini S. Fc-fusion mimetics. Biomater Sci. 2016;4:943–947.
   PubMed Web of Science ®Google Scholar
• Klaus W, Gsell B, Labhardt A, et al. The three-dimensional high resolution structure of human interferon alpha-2a determined by heteronuclear NMR spectroscopy in solution. J Mol Biol. 1997;274:661–675.
   PubMed Web of Science ®Google Scholar
• Cong Y, Pawlisz E, Bryant P, et al. Site-specific PEGylation at histidine tags. Bioconjug Chem. 2012;23:248–263.
   PubMed Web of Science ®Google Scholar
• Lobstein J, Emrich C, Jeans C, et al. SHuffle, a novel Escherichia coli protein expression strain capable of correctly folding disulfide bonded proteins in its cytoplasm. Microb Cell Fact. 2012;11:11.
   PubMed Web of Science ®Google Scholar
• Grace M, Lee S, Bradshaw S, et al. Site of pegylation and polyethylene glycol molecule size attenuate interferon-α antiviral and antiproliferative activities through the JAK/STAT signaling pathway. J Biol Chem. 2005;280:6327–6336.
   PubMed Web of Science ®Google Scholar
• Shaunak S, Godwin A, Choi JW, et al. Site-specific PEGylation of native disulfide bonds in therapeutic proteins. Nat Chem Bio. 2006;2:312–313.
   PubMed Web of Science ®Google Scholar
• Brocchini S, Godwin A, Balan S, et al. Disulfide bridge based PEGylation of proteins. Adv Drug Del Rev. 2008;60:3–12.
   PubMed Web of Science ®Google Scholar