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

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...

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Detalles Bibliográficos
Autores principales: Cao, Guangcan, Gao, Xinyu, Zhan, Yancheng, Wang, Qingguang, Zhang, Zhe, Dimitrov, Dimiter S., Gong, Rui
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2019
Materias:
Report
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6927756/
https://www.ncbi.nlm.nih.gov/pubmed/31795802
http://dx.doi.org/10.1080/19420862.2019.1689027

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6927756/
https://www.ncbi.nlm.nih.gov/pubmed/31795802
http://dx.doi.org/10.1080/19420862.2019.1689027

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