On the relationship between conformation and stability in solid pharmaceutical protein formulations

Biotechnology Letters
A M Klibanov, Jennifer A Schefiliti

Abstract

Long-term stability is critical in the successful development of pharmaceuticals, including macromolecular ones, such as proteins. Due to the relative instability of aqueous solutions of proteins, they are typically stores in a freeze-dried (lyophilized) state. However, proteins reversibly (and sometimes even irreversibly) denature upon lyophilization and consequently adopt conformations markedly distinct from the native ones. This phenomenon may profoundly affect deleterious processes in lyophilized proteins, e.g. moisture-induced aggregation, as illustrated in this review with bovine serum and recombinant human albumins.

Citations

Oct 17, 2006·Pharmaceutical Research·Vikas K Sharma, Alexander M Klibanov
Nov 7, 2009·Proceedings of the National Academy of Sciences of the United States of America·Erik P SundeBertil Halle
May 2, 2013·Biopreservation and Biobanking·Hyun Ju KangBok Ghee Han
Jul 2, 2009·Journal of Pharmaceutical Sciences·Liuquan Lucy Chang, Michael J Pikal
Apr 2, 2005·Nature Reviews. Drug Discovery·Sven Frokjaer, Daniel E Otzen
Dec 29, 2007·Pharmaceutical Development and Technology·Stéphanie PassotMichel Rapaud
Oct 12, 2010·Biomacromolecules·Malvika BihariDavid A Hoagland

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