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Repertoires of aggregation-resistant human antibody domains

Abstract

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.

Type Journal
ISBN 1741-0126 (Print)
Authors Christ, D.;Famm, K.;Winter, G. :
Responsible Garvan Author A/Prof Daniel Christ
Publisher Name PROTEIN ENGINEERING DESIGN & SELECTION
Published Date 2007-01-01
Published Volume 20
Published Issue 8
Published Pages 413-6
Status Published in-print
URL link to publisher's version http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17720749
OpenAccess link to author's accepted manuscript version https://publications.gimr.garvan.org.au/open-access/2184