Dear Marina,

Please read the following text taken from a recent review article entitled "Antibody Aggregation: Insights from Sequence and Structure " published in Antibodies 2016, 5(3), 19; doi:10.3390/antib5030019:

Although the mechanism underlying antibody aggregation is generally not fully understood, the aggregation propensity for a given mAb is a function of solution conditions, such as temperature, pressure, pH, ionic strength and excipients (osmolytes, surfactants). Formulation optimization is commonly used to reduce aggregation. On the other hand, the susceptibility to aggregation is pre-defined by the intrinsic properties of the antibody, including primary sequence and tertiary structure. Protein aggregation needs some degree of conformational distortion or partial unfolding of the native monomer to expose the aggregation-prone residues to form strong inter-molecular interactions. Antibodies usually contain more than one aggregation-prone region (APR). Therefore, by contrast to some simple proteins, in which aggregation occurs in a high cooperativity manner, antibody aggregation usually occurs through several intermediate states, indicating that multi-domain antibody unfolding and aggregation could be understood by analyzing the aggregation of individual domains. The studies of aggregation mechanisms and resistant strategies for antibody domains have inspired the related research of full-length antibodies, although the results obtained from the antibody domains could not always be transferred to the full-sized antibodies. In this paper, we review the impact of sequences and structures on the aggregation of both full length antibodies and antibody domains while discussing aggregation resistance strategies through rational designs.

For more on this topic, please see the publication contained in the following link:

http://www.mdpi.com/2073-4468/5/3/19/htm

Hoping this will be helpful,

Rafik

Thank you very much Rafik.