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

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Abstract

A 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.

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Hussack, G., Keklikian, A., Alsughayyir, J., Hanifi-Moghaddam, P., Arbabi-Ghahroudi, M., Van Faassen, H., … Tanha, J. (2012). A VL single-domain antibody library shows a high-propensity to yield non-aggregating binders. Protein Engineering, Design and Selection, 25(6), 313–318. https://doi.org/10.1093/protein/gzs014

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