Solubility and stability engineering of human VH domains

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DOIResolve DOI: http://doi.org/10.1007/978-1-61779-968-6-21
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TypeArticle
Journal titleMethods in Molecular Biology
ISSN1064-3745
ISBN9781617799679
Volume911
Pages355372; # of pages: 18
Subjectantibody; unclassified drug; vh antibody; disulfide; nanobody; article; priority journal; protein engineering; protein stability; solubility; amino acid sequence; chemistry; complementarity determining region; gene expression; genetics; human; isolation and purification; molecular cloning; molecular genetics; mutation; plasmid; protein engineering; temperature; Amino Acid Sequence; Cloning, Molecular; Complementarity Determining Regions; Disulfides; Gene Expression; Humans; Molecular Sequence Data; Mutation; Plasmids; Protein Engineering; Protein Stability; Single-Domain Antibodies; Solubility; Temperature
AbstractSolubility and stability are amongst the factors contributing to the therapeutic efficacy of biologics. Human antibody heavy chain variable domains, VHs, are one class of biologics; improving VH biophysical properties is the focus of significant protein engineering efforts. Here, we describe an efficacy engineering approach which involves the introduction of a disulfide linkage in the VH core and which improves both VH solubility and stability. More specifically, we describe protocols for generation of disulfide engineered human VHs and their characterization in terms of disulfide linkage formation, non-aggregation, and stability. Our solubility/stability engineering approach may be applied to other VHs. © 2012 Springer Science+Business Media, LLC.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC); NRC Institute for Biological Sciences (IBS-ISB)
Peer reviewedYes
NPARC number21269471
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Record identifier60c55c9c-7090-43c2-a0d6-ce2d3279073d
Record created2013-12-12
Record modified2016-05-09
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