Abolition of aggregation of CH2 domain of human IgG1 when combining glycosylation and protein stabilization

The CH2 domain is a critical element of the human Immunoglobulin G (IgG) constant region. Although least stable in IgG, it also promising scaffold candidate for developing novel therapeutic approaches. Recently, we succeeded preparing glycosylated and non-glycosylated host organism Pichia pastoris. Herein, verified that glycosylation decreased both, its tendency to aggregate immunogenicity mice, suggesting aggregation are related. In addition, have produced P. pastoris stabilized version with without glycan, their propensity evaluated. We found stabilization alone significantly domain. Moreover, combination completely suppressed behavior. Since protein related immunogenicity, eliminate behavior could be fruitful strategy generate immunoglobulin scaffolds.