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Current Pharmaceutical Biotechnology

Editor-in-Chief

ISSN (Print): 1389-2010
ISSN (Online): 1873-4316

Application of Vibrational Spectroscopy to the Structural Characterization of Monoclonal Antibody and its Aggregate

Author(s): Cynthia H. Li and Tiansheng Li

Volume 10, Issue 4, 2009

Page: [391 - 399] Pages: 9

DOI: 10.2174/138920109788488950

Price: $65

Abstract

Aggregation is often the major issue during formulation and manufacturing development of therapeutic proteins, in particular human monoclonal antibody. Currently, there is a lack of structural information of aggregates of such large protein as human antibodies, due to the large molecular sizes of the aggregates. In this article, we shall discuss the application of vibrational spectroscopies including FT-IR, Raman and Raman Optical Activity (ROA), to characterize the structures of various types of monoclonal antibody aggregates formed under different stresses. Two different classes of human monoclonal antibodies, namely IgG1 and IgG2, have been subjected to this structural investigation. The common stresses leading to antibody aggregation, mis-folding or unfolding during manufacturing and formulation include exposure to acidic pHs, heat and shear stress. The effect of different types of stresses on the structure and aggregate formation of human monoclonal antibodies has been investigated by employing vibrational spectroscopy. While data present only monoclonal antibody, the same technology can be used for any protein aggregates.


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