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Article

An engineered human IgG1 CH2 domain with decreased aggregation and nonspecific binding.

mAbs - 1 Jan 2000

Cao Guangcan, Gao Xinyu, Zhan Yancheng, Wang Qingguang, Zhang Zhe, Dimitrov Dimiter S, Gong Rui

Abstract excerpt

The immunoglobulin (Ig) CH2 domain is a promising scaffold for the development of candidate therapeutics. We have previously shown that the stability of isolated CH2 could be increased by the introduction of an additional disulfide bond and removal of seven N-terminal residues (m01s). However, both isolated CH2 and m01s aggregate, likely due to the existence of aggregation-prone regions (APRs) that we identified...

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Share to Antigens, Neoplasm
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 31795802
DOI: 10.1080/19420862.2019.1689027
PMCID: PMC6927756

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