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PEDS Advance Access originally published online on August 24, 2007
Protein Engineering Design and Selection 2007 20(8):413-416; doi:10.1093/protein/gzm037
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© The Author 2007. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Short communication

Repertoires of aggregation-resistant human antibody domains

Daniel Christ1,3,4, Kristoffer Famm2 and Greg Winter1,2

1Laboratory of Molecular Biology 2 Centre for Protein Engineering, Medical Research Council Centre, Hills Road, Cambridge CB2 2QH, UK 3Present address: Garvan Institute of Medical Research, 384 Victoria Street, Darlinghurst, Sydney, NSW 2010, Australia

4 To whom correspondence should be addressed. E-mail: d.christ{at}garvan.org.au

We recently described a method for the generation of a large human domain antibody repertoire involving combinatorial assembly of CDR building blocks from a smaller repertoire comprising a high frequency of aggregation-resistant antibody domains. Here we show that the frequency of aggregation-resistant domains in the combinatorial repertoire remained high. Furthermore, one of the antigen-binding domains selected from the combinatorial repertoire retained its binding properties through 25 cycles of thermal denaturation, suggesting that antibody domains can be created that rival the heat-resistance of thermophilic proteins such as Taq polymerase.

Keywords: combinatorial repertoire/molecular evolution/phage display/protein aggregation

Received June 18, 2007; revised June 18, 2007; accepted June 22, 2007.


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