Have a personal or library account? Click to login
Alternative buffer systems in biopharmaceutical formulations and their effect on protein stability Cover

Alternative buffer systems in biopharmaceutical formulations and their effect on protein stability

Acta Pharmaceutica
Volume 74 (2024): Issue 3 (September 2024)
By:
Open Access
|Sep 2024

References

  1. G. Walsh and E. Walsh, Biopharmaceutical benchmarks 2022, <em>Nat. Biotechnol.</em> <bold>40</bold> (2022) 1722–1760; <ext-link ext-link-type="uri" xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="<a href="https://doi.org/10.1038/s41587-022-01582-x" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">https://doi.org/10.1038/s41587-022-01582-x</a>">https://doi.org/10.1038/s41587-022-01582-x</ext-link>
    Search in Google ScholarBack to article
  2. N. C. Pace and C. Tanford, Thermodynamics of the unfolding of β-lactoglobulin A in aqueous urea solutions between 5 and 55°, <em>Biochemistry</em> <bold>7</bold> (1968) 198–208; <ext-link ext-link-type="uri" xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="<a href="https://doi.org/10.1021/bi00841a025" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">https://doi.org/10.1021/bi00841a025</a>">https://doi.org/10.1021/bi00841a025</ext-link>
    Search in Google ScholarBack to article
  3. F. Jameel and S. Hershenson, <em>Formulation and Process Development Strategies for Manufacturing Biopharmaceuticals,</em> John Wiley &amp; Sons, New Jersey 2002, pp. 69–105.
    Search in Google ScholarBack to article
  4. L. O. Narhi, J. Schmit, K. Bechtold-Peters and D. Sharma, Classification of protein aggregates, <em>J. Pharm. Sci.</em> <bold>101</bold> (2012) 493–498; <ext-link ext-link-type="uri" xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="<a href="https://doi.org/10.1002/jps.22790" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">https://doi.org/10.1002/jps.22790</a>">https://doi.org/10.1002/jps.22790</ext-link>
    Search in Google ScholarBack to article
  5. S. Hermeling, D. J. A. Crommelin, H. Schellekens and W. Jiskoot, Structure-immunogenicity relationships of therapeutic proteins, <em>Pharm. Res.</em> <bold>21</bold> (2004) 897–903; <ext-link ext-link-type="uri" xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="<a href="https://doi.org/10.1023/B:PHAM.0000029275.41323.a6" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">https://doi.org/10.1023/B:PHAM.0000029275.41323.a6</a>">https://doi.org/10.1023/B:PHAM.0000029275.41323.a6</ext-link>
    Search in Google ScholarBack to article
  6. A. Braun, L. Kwee, M. A. Labow and J. Alsenz, Protein aggregates seem to play a key role among the parameters influencing the antigenicity of interferon alpha (IFN-α) in normal and transgenic mice, <em>Pharm. Res.</em> (1997) 1472–1478; <ext-link ext-link-type="uri" xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="<a href="https://doi.org/10.1023/A:1012193326789" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">https://doi.org/10.1023/A:1012193326789</a>">https://doi.org/10.1023/A:1012193326789</ext-link>
    Search in Google ScholarBack to article
  7. Y. Le Basle, P. Chennell, N. Tokhadze, A. Astier and V. Sautou, Physicochemical stability of monoclonal antibodies: A review, <em>J. Pharm. Sci.</em> <bold>109</bold> (2020) 169–190; <ext-link ext-link-type="uri" xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="<a href="https://doi.org/10.1016/j.xphs.2019.08.009" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">https://doi.org/10.1016/j.xphs.2019.08.009</a>">https://doi.org/10.1016/j.xphs.2019.08.009</ext-link>
    Search in Google ScholarBack to article
  8. E. Y. Chi, S. Krishnan, T. W. Randolph and J. F. Carpenter, Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation, <em>Pharm. Res.</em> <bold>20</bold> (2003) 1325–1336; <ext-link ext-link-type="uri" xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="<a href="https://doi.org/10.1023/A:1025771421906" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">https://doi.org/10.1023/A:1025771421906</a>">https://doi.org/10.1023/A:1025771421906</ext-link>
    Search in Google ScholarBack to article
  9. E. Y. Chi, Excipients and their effects on the quality of biologics, <em>Aaps</em> <bold>1</bold> (2012) 1–12.
    Search in Google ScholarBack to article
  10. E. Proksch, Buffering capacity, <em>Curr. Probl. Dermatology</em> <bold>54</bold> (2018) 11–18; <ext-link ext-link-type="uri" xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="<a href="https://doi.org/10.1159/000489513" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">https://doi.org/10.1159/000489513</a>">https://doi.org/10.1159/000489513</ext-link>
    Search in Google ScholarBack to article
  11. E. T. Urbansky and M. R. Schock, Understanding, deriving, and computing buffer capacity, <em>J. Chem. Educ.</em> <bold>77</bold> (2000) 1640–1644; <ext-link ext-link-type="uri" xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="<a href="https://doi.org/10.1021/ed077p1640" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">https://doi.org/10.1021/ed077p1640</a>">https://doi.org/10.1021/ed077p1640</ext-link>
    Search in Google ScholarBack to article
  12. B. N. Dominy, D. Perl, F. X. Schmid and C. L. Brooks, The effects of ionic strength on protein stability: The cold shock protein family, <em>J. Mol. Biol.</em> <bold>319</bold> (2002) 541–554; <ext-link ext-link-type="uri" xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="<a href="https://doi.org/10.1016/S0022-2836(02)00259-0" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">https://doi.org/10.1016/S0022-2836(02)00259-0</a>">https://doi.org/10.1016/S0022-2836(02)00259-0</ext-link>
    Search in Google ScholarBack to article
  13. S. O. Ugwu and A. P. Shireesh, The effect of buffers on protein conformational stability, <em>Pharm. Technol.</em> <bold>81</bold> (2004) 339–352; <ext-link ext-link-type="uri" xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="<a href="https://doi.org/10.1016/j.saa.2011.06.021" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">https://doi.org/10.1016/j.saa.2011.06.021</a>">https://doi.org/10.1016/j.saa.2011.06.021</ext-link>
    Search in Google ScholarBack to article
  14. T. J. Zbacnik, R. E. Holcomb, D. S. Katayama, B. M. Murphy, R. W. Payne, R. C. Coccaro, G. J. Evans, J. E. Matsuura, C. S. Henry and M. C. Manning, Role of buffers in protein formulations, <em>J. Pharm. Sci.</em> <bold>106</bold> (2017) 713–733; <ext-link ext-link-type="uri" xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="<a href="https://doi.org/10.1016/j.xphs.2016.11.014" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">https://doi.org/10.1016/j.xphs.2016.11.014</a>">https://doi.org/10.1016/j.xphs.2016.11.014</ext-link>
    Search in Google ScholarBack to article
  15. R. N. Goldberg, N. Kishore and R. M. Lennen, Thermodynamic quantities for the ionization reactions of buffers, <em>J. Phys. Chem. Ref. Data</em> <bold>31</bold> (2002) 231–370; <ext-link ext-link-type="uri" xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="<a href="https://doi.org/10.1063/1.1416902" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">https://doi.org/10.1063/1.1416902</a>">https://doi.org/10.1063/1.1416902</ext-link>
    Search in Google ScholarBack to article
  16. K. C. Waterman, R. C. Adami, K. M. Alsante, J. Hong, M. S. Landis, F. Lombardo and C. J. Roberts, Stabilization of pharmaceuticals to oxidative degradation, <em>Pharm. Dev. Technol.</em> <bold>7</bold> (2002) 1–32; <ext-link ext-link-type="uri" xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="<a href="https://doi.org/10.1081/PDT-120002237" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">https://doi.org/10.1081/PDT-120002237</a>">https://doi.org/10.1081/PDT-120002237</ext-link>
    Search in Google ScholarBack to article
  17. Y. H. Kim and W. E. Stites, Excluded volume effects upon protein stability in covalently crosslinked proteins with variable linker lengths, <em>Bone</em> <bold>23</bold> (2011) 1–7; <ext-link ext-link-type="uri" xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="<a href="https://doi.org/10.1021/bi800297j" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">https://doi.org/10.1021/bi800297j</a>">https://doi.org/10.1021/bi800297j</ext-link>
    Search in Google ScholarBack to article
  18. C. Du, G. Barnett, A. Borwankar, A. Lewandowski, N. Singh, S. Ghose, M. Borys and Z. J. Li, Protection of therapeutic antibodies from visible light induced degradation: Use safe light in manufacturing and storage, <em>Eur. J. Pharm. Biopharm.</em> <bold>127</bold> (2018) 37–43; <ext-link ext-link-type="uri" xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="<a href="https://doi.org/10.1016/j.ejpb.2018.02.007" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">https://doi.org/10.1016/j.ejpb.2018.02.007</a>">https://doi.org/10.1016/j.ejpb.2018.02.007</ext-link>
    Search in Google ScholarBack to article
  19. M. Lei, C. Quan, Y. J. Wang, Y. H. Kao and C. Schöneich, Light-induced covalent buffer adducts to histidine in a model protein, <em>Pharm. Res.</em> <bold>35</bold> (2018); <ext-link ext-link-type="uri" xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="<a href="https://doi.org/10.1007/s11095-017-2339-4" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">https://doi.org/10.1007/s11095-017-2339-4</a>">https://doi.org/10.1007/s11095-017-2339-4</ext-link>
    Search in Google ScholarBack to article
  20. S. D. Stroop, D. M. Conca, R. P. Lundgard, M. E. Renz, L. M. Peabody and S. D. Leigh, Photosensitizers form in histidine buffer and mediate the photodegradation of a monoclonal antibody, <em>J. Pharm. Sci.</em> <bold>100</bold> (2011) 5142–5155; <ext-link ext-link-type="uri" xmlns:xlink="http://www.w3.org/1999/xlink" xlink:href="<a href="https://doi.org/10.1002/jps.22714" target="_blank" rel="noopener noreferrer" class="text-signal-blue hover:underline">https://doi.org/10.1002/jps.22714</a>">https://doi.org/10.1002/jps.22714</ext-link>
    Search in Google ScholarBack to article
DOI: https://doi.org/10.2478/acph-2024-0022 | Journal eISSN: 1846-9558 | Journal ISSN: 1330-0075
Journal RSS Feed
Language: English
Page range: 479 - 493
Accepted on: May 2, 2024
Published on: Sep 14, 2024
Published by: Croatian Pharmaceutical Society
In partnership with: Paradigm Publishing Services
Publication frequency: 4 times per year
Keywords:
biopharmaceuticals,
buffer,
stress,
aggregates,
alternative buffers,
stability
Related subjects:
Pharmacy,
Pharmacy, other

© 2024 Blaž Lebar, Mitja Zidar, Janez Mravljak, Roman Šink, Aleš Žula, Stane Pajk, published by Croatian Pharmaceutical Society
This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 License.

Previous articleVolume 74 (2024): Issue 3 (September 2024)Next article