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Ecker DM, Jones SD, Levine HL. The therapeutic monoclonal antibody market. MAbs. 2015;7(1):9–14. https://doi.org/10.4161/19420862.2015.989042. Goswami S, Wang W, Arakawa T, Ohtake S. Developments and challenges for mAb-based therapeutics. Antibodies. 2013;2(3):452–500. Razinkov VI, Treuheit MJ, Becker GW. Accelerated formulation development of monoclonal antibodies (mAbs) and mAb-based modalities: review of methods and tools. J Biomol Screen. 2015;20(4):468–83. https://doi.org/10.1177/1087057114565593. Jiskoot W, Randolph TW, Volkin DB, Russell Middaugh C, Schöneich C, Winter G, et al. Protein instability and immunogenicity: roadblocks to clinical application of injectable protein delivery systems for sustained release. J Pharm Sci. 2012;101(3):946–54. https://doi.org/10.1002/jps.23018. Shire SJ, Shahrokh Z, Liu J. Challenges in the development of high protein concentration formulations. J Pharm Sci. 2004;93(6):1390–402. https://doi.org/10.1002/jps.20079. Philo JS, Arakawa T. Mechanisms of protein aggregation. Curr Pharm Biotechnol. 2009;10(4):348–51. https://doi.org/10.2174/138920109788488932. Alford JR, Kendrick BS, Carpenter JF, Randolph TW. High concentration formulations of recombinant human interleukin-1 receptor antagonist: II. Aggregation kinetics. J Pharm Sci. 2008;97(8):3005–21. https://doi.org/10.1002/jps.21205. Nishi H, Miyajima M, Nakagami H, Noda M, Uchiyama S, Fukui K. Phase separation of an IgG1 antibody solution under a low ionic strength condition. Pharm Res. 2010;27(7):1348–60. https://doi.org/10.1007/s11095-010-0125-7. Wei JY, Bou-Assaf GM, Houde D, Weiskopf A. Technical decision-making with higher order structure data: detecting reversible concentration-dependent self-Association in a Monoclonal Antibody and a preliminary investigation to eliminate it. J Pharm Sci. 2015;104(11):3984–9. https://doi.org/10.1002/jps.24616. Esfandiary R, Parupudi A, Casas-Finet J, Gadre D, Sathish H. Mechanism of reversible self-association of a monoclonal antibody: role of electrostatic and hydrophobic interactions. J Pharm Sci. 2015;104(2):577–86. https://doi.org/10.1002/jps.24237. Sule SV, Cheung JK, Antochshuk V, Bhalla AS, Narasimhan C, Blaisdell S, et al. Solution pH that minimizes self-association of three monoclonal antibodies is strongly dependent on ionic strength. Mol Pharm. 2012 Apr 2;9(4):744–51. https://doi.org/10.1021/mp200448j Epub 2012 Feb 17. Geoghegan JC, Fleming R, Damschroder M, Bishop SM, Sathish HA, Esfandiary R. Mitigation of reversible self-association and viscosity in a human IgG1 monoclonal antibody by rational, structure-guided Fv engineering. MAbs. 2016;8(5):941–50. https://doi.org/10.1080/19420862.2016.1171444. Hopkins MM, Lambert CL, Bee JS, Parupudi A, Bain DL. Determination of interaction parameters for reversibly self-associating antibodies: a comparative analysis. J Pharm Sci. 2018;107(7):1820–30. https://doi.org/10.1016/j.xphs.2018.03.011. Tanford C. Physical chemistry of macromolecules. New York: Wiley; 1961. Rowe AJ. The concentration dependence of transport processes: a general description applicable to the sedimentation, translational diffusion, and viscosity coefficients of macromolecular solutes. Biopolymers. 1977;16:2595–611. https://doi.org/10.1002/bip.1977.360161202\. Cole JL, Correia JJ, Stafford WF. The use of analytical sedimentation velocity to extract thermodynamic linkage. Biophys Chem. 2011;159(1):120–8. https://doi.org/10.1016/j.bpc.2011.05.014. Correia JJ, Wright RT, Sherwood PJ, Stafford WF. Analysis of nonideality: insights from high concentration simulations of sedimentation velocity data. Eur Biophys J. 2020 Dec;49(8):687–700. https://doi.org/10.1007/s00249-020-01474-5. Epub 2020 Nov 6. Esfandiary R, Hayes DB, Parupudi A, Casas-Finet J, Bai S, Samra HS, et al. A systematic multitechnique approach for detection and characterization of reversible self-association during formulation development of therapeutic antibodies. J Pharm Sci. 2013;102(9):3089–99. https://doi.org/10.1002/jps.23654. Arora J, Hu Y, Esfandiary R, et al. Charge-mediated Fab-Fc interactions in an IgG1 antibody induce reversible self-association, cluster formation, and elevated viscosity. MAbs. 8(8):1561–74. https://doi.org/10.1080/19420862.2016.1222342. Hu Y, Arora J, Joshi SB, Esfandiary R, Middaugh CR, Weis DD, et al. Characterization of excipient effects on reversible self-association, backbone flexibility, and solution properties of an IgG1 monoclonal antibody at high concentrations: part 1. J Pharm Sci. 2020;109(1):340–52. https://doi.org/10.1016/j.xphs.2019.06.005. Hu Y, Toth RT 4th, Joshi SB, et al. Characterization of excipient effects on reversible self-association, backbone flexibility, and solution properties of an IgG1 monoclonal antibody at high concentrations: part 2. J Pharm Sci. 2020;109(1):353–63. https://doi.org/10.1016/j.xphs.2019.06.001. Arora J, Hickey JM, Majumdar R, Esfandiary R, Bishop SM, Samra HS, et al. Hydrogen exchange mass spectrometry reveals protein interfaces and distant dynamic coupling effects during the reversible self-association of an IgG1 monoclonal antibody. MAbs. 2015;7(3):525–39. https://doi.org/10.1080/19420862.2015.1029217. Hayes D, Laue T, Philo J. Program SEDNTERP: Sedimentation interpretation program. Durham, NH: University of New Hampshire;1995, www.jphilo.mailway.com/download.htm#sednterp Stafford WF 3rd. Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile. Anal Biochem. 1992;203(2):295–301. https://doi.org/10.1016/0003-2697(92)90316-y. Philo JS. Improved methods for fitting sedimentation coefficient distributions derived by time-derivative techniques. Anal Biochem. 2006;354(2):238–46. https://doi.org/10.1016/j.ab.2006.04.053. Stafford WF, Sherwood PJ. Analysis of heterologous interacting systems by sedimentation velocity: curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and kinetic constants. Biophys Chem. 2004;108(1–3):231–43. https://doi.org/10.1016/j.bpc.2003.10.028. Claverie JM, Dreux H, Cohen R. Sedimentation of generalized systems of interacting particles. I. Solution of systems of complete Lamm equations. Biopolymers. 1975;14(8):1685–700. https://doi.org/10.1002/bip.1975.360140811. Claverie JM. Sedimentation of generalized systems of interacting particles. III. Concentration-dependent sedimentation and extension to other transport methods. Biopolymers. 1976;15(5):843–57. https://doi.org/10.1002/bip.1976.360150504. Sorret LL, DeWinter MA, Schwartz DK, Randolph TW. Challenges in predicting protein-protein interactions from measurements of molecular diffusivity. Biophys J. 2016 Nov 1;111(9):1831–1842. https://doi.org/10.1016/j.bpj.2016.09.018. Correia JJ. Analysis of weight average sedimentation velocity data. Methods Enzymol. 2000;321:81–100. https://doi.org/10.1016/s0076-6879(00)21188-9. Sontag CA, Stafford WF, Correia JJ. A comparison of weight average and direct boundary fitting of sedimentation velocity data for indefinite polymerizing systems. Biophys Chem. 2004;108(1–3):215–30. https://doi.org/10.1016/j.bpc.2003.10.029. Correia JJ, Stafford WF. Extracting equilibrium constants from kinetically limited reacting systems. Methods Enzymol. 2009;455:419–46. https://doi.org/10.1016/S0076-6879(08)04215-8. Creeth JM, Knight CG. On the estimation of the shape of macromolecules from sedimentation and viscosity measurements. Biochim Biophys Acta. 1965;102(2):549–58. https://doi.org/10.1016/0926-6585(65)90145-7. Yang D, Correia JJ, Stafford WF III, et al. Weak IgG self- and hetero-association characterized by fluorescence analytical ultracentrifugation. Protein Sci. 2018;27(7):1334–48. https://doi.org/10.1002/pro.3422. Wright RT, Hayes DB, Stafford WF, Sherwood PJ, Correia JJ. Characterization of therapeutic antibodies in the presence of human serum proteins by AU-FDS analytical ultracentrifugation. Anal Biochem. 2018 Jun;550:72–83. https://doi.org/10.1016/j.ab.2018.04.002. Diebolder CA, Beurskens FJ, de Jong RN, Koning RI, Strumane K, Lindorfer MA, et al. Complement is activated by IgG hexamers assembled at the cell surface. Science. 2014;343(6176):1260–3. https://doi.org/10.1126/science.1248943. de la Torre JG, Echenique Gdel R, Ortega A. Improved calculation of rotational diffusion and intrinsic viscosity of bead models for macromolecules and nanoparticles. J Phys Chem B. 2007;111(5):955–61. https://doi.org/10.1021/jp0647941. Lin J, Lucius AL. Examination of the dynamic assembly equilibrium for E. coli ClpB. Proteins. 2015;83(11):2008–24. https://doi.org/10.1002/prot.24914. Philo JS. Characterizing the aggregation and conformation of protein therapeutics. American Biotechnology Laboratory. 2003;21(11):22–6. Johnson ML. Parameter correlations while curve fitting. Methods Enzymol. 2000;321:424–46. https://doi.org/10.1016/s0076-6879(00)21207-x. Horn JR, Russell D, Lewis EA, Murphy KP. Van't Hoff and calorimetric enthalpies from isothermal titration calorimetry: are there significant discrepancies? Biochemistry. 2001;40(6):1774–8. https://doi.org/10.1021/bi002408e. Ross PD, Subramanian S. Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry. 1981;20(11):3096–102. https://doi.org/10.1021/bi00514a017. Winzor DJ, Jackson CM. Interpretation of the temperature dependence of equilibrium and rate constants. J Mol Recognit. 2006;19(5):389–407. https://doi.org/10.1002/jmr.799.