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PEDS Advance Access published online on August 18, 2006
Protein Engineering Design and Selection, doi:10.1093/protein/gzl032
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© The Author 2006. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org
Received July 3, 2006
Accepted July 10, 2006

Short Communication

Engineering aggregation-resistant proteins by directed evolution

K. Famm 1 and G. Winter 2 *

1 Centre for Protein Engineering, Medical Research Council Centre, Hills Road, Cambridge CB2 2QH, UK
2 Centre for Protein Engineering, Medical Research Council Centre, Hills Road, Cambridge CB2 2QH, UK; Laboratory of Molecular Biology, Medical Research Council Centre, Hills Road, Cambridge CB2 2QH, UK

* To whom correspondence should be addressed.
G. Winter, E-mail: winter{at}mrc-lmb.cam.c.uk


  Abstract

A method was recently described for selecting aggregation-resistant antibody domains. A repertoire of domains displayed on filamentous bacteriophage were heated/cooled and selected for binding to the affinity ligand protein A specific for the folded domains. Here we describe a generalization of the method based on the selection for retained phage infectivity and for the binding of an appended sequence tag, and applicable to any protein displayable in multivalent form on phage.

Keywords: directed evolution; protein aggregation; phage display.
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