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Solubility and stability engineering of human VH domains

Par Conseil national de recherches du Canada

DOITrouver le DOI : https://doi.org/10.1007/978-1-61779-968-6-21
AuteurRechercher : 1; Rechercher : 1; Rechercher : 1
Affiliation
  1. Conseil national de recherches du Canada. Institut des sciences biologiques du CNRC
FormatTexte, Article
Sujetantibody; unclassified drug; vh antibody; disulfide; nanobody; protein engineering; protein stability; solubility; amino acid sequence; chemistry; complementarity determining region; gene expression; genetics; isolation and purification; molecular cloning; molecular genetics; mutation; plasmid; protein engineering; temperature; Amino Acid Sequence; Cloning, Molecular; Complementarity Determining Regions; Disulfides; Gene Expression; Molecular Sequence Data; Mutation; Plasmids; Protein Engineering; Protein Stability; Single-Domain Antibodies; Solubility; Temperature
Résumé
Solubility 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.
Date de publication
Dans
  • Methods in Molecular Biology 911 (2012) : 355–372.
Langueanglais
Publications évaluées par des pairsOui
Numéro NPARC21269471
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Identificateur de l’enregistrement60c55c9c-7090-43c2-a0d6-ce2d3279073d
Enregistrement créé2013-12-12
Enregistrement modifié2020-04-21
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