Lyophilised protein formulations as a patient-centric dosage form: A contribution toward sustainability paradigm

1 M. G. Tovey and C. Lallemand, Immunogenicity and other problems associated with the use of biopharmaceuticals, Ther. Adv. Drug Saf. 2(3) (2011) 113–128; https://doi.org/10.1177/2042098611406318 Search in Google Scholar

2 L. Kagan, M. R. Turner, S. V. Balu-Iyer and D. E. Mager, Subcutaneous absorption of monoclonal antibodies: Role of dose, site of injection, and injection volume on rituximab pharmacokinetics in rats, Pharm. Res. 29(2) (2012) 490–499; https://doi.org/10.1007/s11095-011-0578-3 Search in Google Scholar

3 M. Viola, J. Sequeira, R. Seiça, F. Veiga, J. Serra, A. C. Santos and A. J. Ribeiro, Subcutaneous delivery of monoclonal antibodies: How do we get there?, J. Controll. Release 286 (2018) 301–314; https://doi.org/10.1016/j.jconrel.2018.08.001 Search in Google Scholar

4 P. Garidel, B. Pevestorf and S. Bahrenburg, Stability of buffer-free freeze-dried formulations: A feasibility study of a monoclonal antibody at high protein concentrations, Eur. J. Pharm. Biopharm. 97 (2015) 125–139; https://doi.org/10.1016/j.ejpb.2015.09.017 Search in Google Scholar

5 S. J. Shire, Z. Shahrokh and J. Liu, Challenges in the development of high protein concentration formulations, J. Pharm. Sci. 93(6) (2004) 1390–402; https://doi.org/10.1002/jps.20079 Search in Google Scholar

6 M. Bjelošević, A. Zvonar Pobirk, O. Planinšek and P. Ahlin Grabnar, Excipients in freeze-dried biopharmaceuticals: Contributions toward formulation stability and lyophilisation cycle optimisation, Int. J. Pharm. 576 (2020) Article ID 119029 (12 pages); https://doi.org/10.1016/j.ijpharm.2020.119029 Search in Google Scholar

7 X. (Charlie) Tang and M. J. Pikal, Design of freeze-drying processes for pharmaceuticals: Practical advice, Pharm. Res. 21(2) (2004) 191–200; https://doi.org/10.1023/B:PHAM.0000016234.73023.75 Search in Google Scholar

8 M. Bjelošević and P. Ahlin Grabnar, Effects of monoclonal antibody concentration and type of bulking agent on critical quality attributes of lyophilisates, J. Drug Deliv. Sci. Technol. 63 (2021) Article ID 102510 (10 pages); https://doi.org/10.1016/j.jddst.2021.102510 Search in Google Scholar

9 D. Dixon, S. Tchessalov, A. Barry and N. Warne, The impact of protein concentration on mannitol and sodium chloride crystallinity and polymorphism upon lyophilization, J. Pharm. Sci. 98(9) (2009) 3419–3429; https://doi.org/10.1002/jps.21537 Search in Google Scholar

10 X. Li and S. L. Nail, Kinetics of glycine crystallization during freezing of sucrose/glycine excipient systems, J. Pharm. Sci. 94(3) (2005) 625–631; https://doi.org/10.1002/jps.20286 Search in Google Scholar

11 M. Anko, M. Bjelošević, O. Planinšek, U. Trstenjak, M. Logar, P. Ahlin Grabnar and B. Brus, The formation and effect of mannitol hemihydrate on the stability of monoclonal antibody in the lyophilized state, Int. J. Pharm. 564 (2019) 106–116; https://doi.org/10.1016/j.ijpharm.2019.04.044 Search in Google Scholar

12 J. H. Gu, R. Qian, R. Chou, P. V. Bondarenko and M. Goldenberg, Rotational rheology of bovine serum albumin solutions: Confounding effects of impurities, mechanistic considerations and potential implications on protein formulation development, Pharm. Res. 35(157) (2018) 1–12; https://doi.org/10.1007/s11095-018-2423-4 Search in Google Scholar

13 A. D. Gonçalves, C. Alexander, C. J. Roberts, S. G. Spain, S. Uddin and S. Allen, The effect of protein concentration on the viscosity of a recombinant albumin solution formulation, RSC Adv. 6(18) (2016) 15143–15154; https://doi.org/10.1039/C5RA21068B Search in Google Scholar

14 J. Li, Y. Cheng, X. Chen and S. Zheng, Impact of electroviscous effect on viscosity in developing highly concentrated protein formulations: Lessons from non-protein charged colloids, Int. J. Pharm. 108 (2019) 1423–143; https://doi.org/10.1016/j.ijpx.2018.100002 Search in Google Scholar

15 V. Sharma, A. Jaishankar, Y. C. Wang and G. H. McKinley, Rheology of globular proteins: Apparent yield stress, high shear rate viscosity and interfacial viscoelasticity of bovine serum albumin solutions, Soft Matter 7 (2011) Article ID 5150 (11 pages); https://doi.org/10.1039/C0SM01312A Search in Google Scholar

16 Z. Zhang and Y. Liu, Recent progresses of understanding the viscosity of concentrated protein solutions, Nanotechnol. Sep. Eng. 16 (2017) 48–55; https://doi.org/10.1016/j.coche.2017.04.001 Search in Google Scholar

17 S. M. Patel, S. L. Nail, M. J. Pikal, R. Geidobler, G. Winter, A. Hawe, J. Davagnino and S. Rambhatla Gupta, Lyophilised drug product cake appearance: What is acceptable?, J. Pharm. Sci. 106(7) (2017) 1706–1721; https://doi.org/10.1016/j.xphs.2017.03.014 Search in Google Scholar

18 M. Bjelošević, K. Bolko Seljak, U. Trstenjak, M. Logar, B. Brus and P. Ahlin Grabnar, Aggressive conditions during primary drying as a contemporary approach to optimise freeze-drying cycles of biopharmaceuticals, Eur. J. Pharm. Sci. 122 (2018) 292–302; https://doi.org/10.1016/j.ejps.2018.07.016 Search in Google Scholar

19 T. Werk, J. Huwyler, M. Hafner, J. Luemkemann and H.-C. Mahler, An impedance-based method to determine reconstitution time for freeze-dried pharmaceuticals, J. Pharm. Sci. 104(9) (2015) 2948–2955; https://doi.org/10.1002/jps.24443 Search in Google Scholar

20 W. Cao, S. Krishnan, M. Speed Ricci, L. Y. Shih, D. Liu, J. H. Gu and F. Jameel, Rational design of lyophilized high concentration protein formulations-mitigating the challenge of slow reconstitution with multidisciplinary strategies, Eur. J. Pharm. Biopharm. 85(2) (2013) 287–293; https://doi.org/10.1016/j.ejpb.2013.05.001 Search in Google Scholar

21 S. S. Kulkarni, R. Suryanarayanan, J. V. Rinella and R. H. Bogner, Mechanisms by which crystalline mannitol improves the reconstitution time of high concentration lyophilized protein formulations, Eur. J. Pharm. Biopharm. 131 (2018) 70–81; https://doi.org/10.1016/j.ejpb.2018.07.022 Search in Google Scholar

22 C. J. Roberts, Protein aggregation and its impact on product quality, Curr. Opin. Biotechnol. 30 (2014) 211–217; https://doi.org/10.1016/j.copbio.2014.08.001 Search in Google Scholar

23 G. Yohannes, S. K. Wiedmer, M. Elomaa, M. Jussila, V. Aseyev and M.-L. Riekkola, Thermal aggregation of bovine serum albumin studied by asymmetrical flow field-flow fractionation, Anal. Chim. Acta. 675(2) (2010) 191–198; https://doi.org/10.1016/j.aca.2010.07.016 Search in Google Scholar

24 Y. Li, G. Yang and Z. Mei, Spectroscopic and dynamic light scattering studies of the interaction between pterodontic acid and bovine serum albumin, Acta Pharm. Sin. B. 2(1) (2012) 53–59; https://doi.org/10.1016/j.apsb.2011.12.001 Search in Google Scholar