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Research Article

Formation of multimeric antibodies for self-delivery of active monomers

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Pages 199-208 | Received 16 Aug 2016, Accepted 25 Sep 2016, Published online: 03 Feb 2017

References

  • Aizenshtein E, Yosipovich R, Kvint M, et al. (2016). Practical aspects in the use of passive immunization as an alternative to attenuated viral vaccines. Vaccine 34:2513–18
  • Ansari MJ, Anwer MK, Jamil S, et al. (2016). Enhanced oral bioavailability of insulin-loaded solid lipid nanoparticles: pharmacokinetic bioavailability of insulin-loaded solid lipid nanoparticles in diabetic rats. Drug Deliv 23:1972–9
  • Arosio P, Barolo G, Muller-Spath T, et al. (2011). Aggregation stability of a monoclonal antibody during downstream processing. Pharm Res 28:1884–94
  • Arosio P, Rima S, Morbidelli M. (2013). Aggregation mechanism of an IgG2 and two IgG1 monoclonal antibodies at low pH: from oligomers to larger aggregates. Pharm Res 30:641–54
  • Babor M, Mandell DJ, Kortemme T. (2011). Assessment of flexible backbone protein design methods for sequence library prediction in the therapeutic antibody Herceptin–HER2 interface. Protein Sci 20:1082–9
  • Brummitt RK, Nesta DP, Chang L, et al. (2011a). Nonnative aggregation of an IgG1 antibody in acidic conditions: part 1. Unfolding, colloidal interactions, and formation of high-molecular-weight aggregates. J Pharm Sci 100:2087–103
  • Brummitt RK, Nesta DP, Chang L, et al. (2011b). Nonnative aggregation of an IgG1 antibody in acidic conditions, part 2: nucleation and growth kinetics with competing growth mechanisms. J Pharm Sci 100:2104–19
  • Chames P, Van Regenmortel M, Weiss E, Baty D. (2009). Therapeutic antibodies: successes, limitations and hopes for the future. Br J Pharmacol 157:220–33
  • Danne T, Bolinder J. (2011). New insulins and insulin therapy. Int J Clin Pract Suppl 65:26–30
  • De Mattos-Arruda L, Cortes J. (2012). Advances in first-line treatment for patients with HER-2+ metastatic breast cancer. Oncologist 17:631–44
  • Dekel Y, Glucksam Y, Margalit R. (2010). Novel fibrillar insulin formulations for oral administration: formulation and in vivo studies in diabetic mice. J Control Release 143:128–35
  • Friedman R, Caflisch A. (2011). Surfactant effects on amyloid aggregation kinetics. J Mol Biol 414:303–12
  • Gazit E. (2002). The “Correctly Folded” state of proteins: is it a metastable state? Angew Chem Int Ed Engl 41:257–9
  • Gimeno MJ, García-Esteo F, García-Honduvilla N, et al. (2002). Polymer controlled drug delivery system for growth hormone. Drug Deliv 9:233–7
  • Horcas I, Fernandez R, Gomez-Rodriguez JM, et al. (2007). WSXM: a software for scanning probe microscopy and a tool for nanotechnology. Rev Sci Instrum 78:013705
  • Hosseinzadeh G, Maghari A, Saboury AA, Moosavi-Movahedi AA. (2016). Unfolding of insulin at the surface of ZnO quantum dots. Int J Biol Macromol 86:169–76
  • Ionescu-Zanetti C, Khurana R, Gillespie JR, et al. (1999). Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy. Proc Natl Acad Sci USA 96:13175–9
  • Jiang D, Rauda I, Han S, et al. (2012). Aggregation pathways of the amyloid β(1–42) peptide depend on its colloidal stability and ordered β-sheet stacking. Langmuir 28:12711–21
  • Jimenez JL, Nettleton EJ, Bouchard M, et al. (2002). The protofilament structure of insulin amyloid fibrils. Proc Natl Acad Sci USA 99:9196–201
  • Jordens S, Adamcik J, Amar-Yuli I, Mezzenga R. (2011). Disassembly and reassembly of amyloid fibrils in water–ethanol mixtures. Biomacromolecules 12:187–93
  • Kardos J, Micsonai A, Pal-Gabor H, et al. (2011). Reversible heat-induced dissociation of β2-microglobulin amyloid fibrils. Biochemistry 50:3211–20
  • Kelly JW. (1996). Alternative conformations of amyloidogenic proteins govern their behavior. Curr Opin Struct Biol 6:11–17
  • Kumar EK, Haque N, Prabhu NP. (2016). Kinetics of protein fibril formation: methods and mechanisms. Int J Biol Macromol. [Epub ahead of print]. doi: 10.1016/j.ijbiomac.2016.06.052
  • Lee EN, Kim YM, Lee HJ, et al. (2005). Stabilizing peptide fusion for solving the stability and solubility problems of therapeutic proteins. Pharm Res 22:1735–46
  • Maji SK, Perrin MH, Sawaya MR, et al. (2009). Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325:328–32
  • Narayanaswamy R, Wang T, Torchilin VP. (2016). Improving peptide applications using nanotechnology. Curr Top Med Chem 16:253–70
  • Nicoud L, Arosio P, Sozo M, et al. (2014a). Kinetic analysis of the multistep aggregation mechanism of monoclonal antibodies. J Phys Chem B 118:10595–606
  • Nicoud L, Jagielski J, Pfister D, et al. (2016). Kinetics of monoclonal antibody aggregation from dilute toward concentrated conditions. J Phys Chem B 120:3267–80
  • Nicoud L, Sozo M, Arosio P, et al. (2014b). Role of cosolutes in the aggregation kinetics of monoclonal antibodies. J Phys Chem B 118:11921–30
  • Nielsen L, Khurana R, Coats A, et al. (2001). Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 40:6036–46
  • Oboroceanu D, Wang L, Brodkorb A, et al. (2010). Characterization of beta-lactoglobulin fibrillar assembly using atomic force microscopy, polyacrylamide gel electrophoresis, and in situ Fourier transform infrared spectroscopy. J Agric Food Chem 58:3667–73
  • Pashley CL, Hewitt EW, Radford SE. (2016). Comparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formation. J Mol Biol 428:631–43
  • Pedersen JS, Otzen DE. (2008). Amyloid – a state in many guises: survival of the fittest fibril fold. Protein Sci 17:2–10
  • Pfohler C, Muller CS, Hasselmann DO, Tilgen W. (2008). Successful desensitization with human insulin in a patient with an insulin allergy and hypersensitivity to protamine: a case report. J Med Case Reports 2:283
  • Rahman S, Van Nguyen S, Icatlo FC Jr, et al. (2013). Oral passive IgY-based immunotherapeutics: a novel solution for prevention and treatment of alimentary tract diseases. Hum Vaccin Immunother 9:1039–48
  • Rajpar SF, Foulds IS, Abdullah A, Maheshwari M. (2006). Severe adverse cutaneous reaction to insulin due to cresol sensitivity. Contact Dermatitis 55:119–20
  • Ramshini H, Parrini C, Relini A, et al. (2011). Large proteins have a great tendency to aggregate but a low propensity to form amyloid fibrils. PLoS One 6:e16075
  • Soreq H, Gazit E. (2008). The structural basis of amyloid formation. Curr Alzheimer Res 5:232
  • Szlachcic A, Zakrzewska M, Otlewski J. (2011). Longer action means better drug: tuning up protein therapeutics. Biotechnol Adv 29:436–41
  • Teng JA, Hou RL, Li DL, et al. (2011). Glargine promotes proliferation of breast adenocarcinoma cell line MCF-7 via AKT activation. Horm Metab Res 43:519–23
  • Thomson NH. (2005a). Imaging the substructure of antibodies with tapping-mode AFM in air: the importance of a water layer on mica. J Microsc 217:193–9
  • Thomson NH. (2005b). The substructure of immunoglobulin G resolved to 25 kDa using amplitude modulation AFM in air. Ultramicroscopy 105:103–10
  • Whittingham JL, Scott DJ, Chance K, et al. (2002). Insulin at pH 2: structural analysis of the conditions promoting insulin fibre formation. J Mol Biol 318:479–90
  • Yosipovich R, Aizenshtein E, Shadmon R, et al. (2015). Overcoming the susceptibility gap between maternal antibody disappearance and auto-antibody production. Vaccine 33:472–8