Optimal charged mutations in the complementarity-determining regions that prevent domain antibody aggregation are dependent on the antibody scaffold

Protein Engineering, Design and Selection

Volumn 27, Issue 2, 2014, Pages 29-39

  Perchiacca, Joseph M ^a   Lee, Christine C ^a   Tessier, Peter M ^a  

^a RENSSELAER POLYTECHNIC INSTITUTE   (United States)

Author keywords

amyloid; CDR; monoclonal; solubility; VH

Indexed keywords

AMYLOID; ANTIBODY AGGREGATION; CDR; COMPLEMENTARITY-DETERMINING REGIONS; MONOCLONAL; POSITIVELY CHARGED; SINGLE-DOMAIN ANTIBODIES; THERAPEUTIC ANTIBODIES;

HYDROPHOBICITY; OPTIMIZATION; SCAFFOLDS; SOLUBILITY;

ANTIBODIES;

ANTIBODY; ANTIBODY SCAFFOLD; NANOBODY; UNCLASSIFIED DRUG;

ANTIBODY AGGREGATION; ANTIBODY ENGINEERING; ANTIGEN BINDING; ARTICLE; BINDING AFFINITY; CIRCULAR DICHROISM; COMPLEMENTARITY DETERMINING REGION; GEL PERMEATION CHROMATOGRAPHY; GENE SYNTHESIS; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DOMAIN; RESTRICTION SITE; SOLUBILITY;

AMYLOID; CDR; MONOCLONAL; SOLUBILITY; VH;

AMINO ACID SEQUENCE; COMPLEMENTARITY DETERMINING REGIONS; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN ENGINEERING; PROTEIN STABILITY; SINGLE-DOMAIN ANTIBODIES; SOLUBILITY;

EID: 84892946282     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzt058     Document Type: Article

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