Phase behavior of an intact monoclonal antibody.

Abstract:

:Understanding protein phase behavior is important for purification, storage, and stable formulation of protein drugs in the biopharmaceutical industry. Glycoproteins, such as monoclonal antibodies (MAbs) are the most abundant biopharmaceuticals and probably the most difficult to crystallize among water-soluble proteins. This study explores the possibility of correlating osmotic second virial coefficient (B(22)) with the phase behavior of an intact MAb, which has so far proved impossible to crystallize. The phase diagram of the MAb is presented as a function of the concentration of different classes of precipitants, i.e., NaCl, (NH4)2SO4, and polyethylene glycol. All these precipitants show a similar behavior of decreasing solubility with increasing precipitant concentration. B(22) values were also measured as a function of the concentration of the different precipitants by self-interaction chromatography and correlated with the phase diagrams. Correlating phase diagrams with B(22) data provides useful information not only for a fundamental understanding of the phase behavior of MAbs, but also for understanding the reason why certain proteins are extremely difficult to crystallize. The scaling of the phase diagram in B(22) units also supports the existence of a universal phase diagram of a complex glycoprotein when it is recast in a protein interaction parameter.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Ahamed T,Esteban BN,Ottens M,van Dedem GW,van der Wielen LA,Bisschops MA,Lee A,Pham C,Thömmes J

doi

10.1529/biophysj.106.098293

subject

Has Abstract

pub_date

2007-07-15 00:00:00

pages

610-9

issue

2

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(07)71312-7

journal_volume

93

pub_type

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