A VL single-domain antibody library shows a high-propensity to yield non-aggregating binders

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DOIResolve DOI: http://doi.org/10.1093/protein/gzs014
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TypeArticle
Journal titleProtein Engineering, Design and Selection
ISSN1741-0126
Volume25
Issue6
Pages313318; # of pages: 6
SubjectAntibody library; Complementarity-determining regions; non-aggregating; Phage display libraries; Single domains; Antibodies; Antigens; Scaffolds; Binders; antibody; bacterial antigen; bacterial protein; bacterial toxin; immunoglobulin light chain; single chain fragment variable antibody; toxB protein, Clostridium difficile; antibody library; antigen expression; article; codon; controlled study; dissociation; enzyme linked immunosorbent assay; human; polyacrylamide gel electrophoresis; priority journal; scanning electron microscopy; solubility; amino acid sequence; antibody affinity; chemistry; genetics; metabolism; molecular cloning; molecular genetics; nucleotide sequence; peptide library; protein binding; Amino Acid Sequence; Antibody Affinity; Antigens, Bacterial; Bacterial Proteins; Bacterial Toxins; Base Sequence; Cloning, Molecular; Enzyme-Linked Immunosorbent Assay; Humans; Immunoglobulin Light Chains; Molecular Sequence Data; Peptide Library; Protein Binding; Single-Chain Antibodies
AbstractA synthetic human VL phage display library, created by the randomization of all complementarity-determining regions (CDRs) in a V L scaffold, was panned against three test antigens to determine the propensity of the library to yield non-aggregating binders. A total of 22 binders were isolated against the test antigens and the majority (20) were monomeric. Thus, human VL repertoires provide an efficient source of non-aggregating binders and represent an attractive alternative to human V H repertoires, which are notorious for containing high proportions of aggregating species. Moreover, the solubility of VLs, in contrast to VHs, appears much less CDR dependent. © The Author 2012. Published by Oxford University Press.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC); NRC Institute for Biological Sciences (IBS-ISB)
Peer reviewedYes
NPARC number21269535
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Record identifier3cce1590-8dbb-4117-8281-e32f3e6de1f7
Record created2013-12-12
Record modified2016-05-09
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