Open AccessApplication of hanging drop technique to optimize human IgG formulations
Author(s) -
Li Guohua,
Kasha Purna C.,
Late Sameer,
Banga Ajay K.
Publication year - 2010
Publication title -
journal of pharmacy and pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 118
eISSN - 2042-7158
pISSN - 0022-3573
DOI - 10.1211/jpp.62.01.0014
Subject(s) - chromatography , chemistry , potassium phosphate , phosphate buffered saline , dynamic light scattering , drop (telecommunication) , size exclusion chromatography , immunoglobulin g , solubility , antibody , biochemistry , materials science , nanotechnology , immunology , organic chemistry , nanoparticle , biology , telecommunications , computer science , enzyme
Objectives The purpose of this work is to assess the hanging drop technique in screening excipients to develop optimal formulations for human immunoglobulin G (IgG). Methods A microdrop of human IgG and test solution hanging from a cover slide and undergoing vapour diffusion was monitored by a stereomicroscope. Aqueous solutions of IgG in the presence of different pH, salt concentrations and excipients were prepared and characterized. Key findings Low concentration of either sodium/potassium phosphate or McIlvaine buffer favoured the solubility of IgG. Addition of sucrose favoured the stability of this antibody while addition of NaCl caused more aggregation. Antimicrobial preservatives were also screened and a complex effect at different buffer conditions was observed. Dynamic light scattering, differential scanning calorimetry and size exclusion chromatography studies were performed to further validate the results. Conclusions In conclusion, hanging drop is a very easy and effective approach to screen protein formulations in the early stage of formulation development.