Repertoires of aggregation-resistant human antibody domains
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.
|Authors||Christ, D.;Famm, K.;Winter, G. :|
|Responsible Garvan Author||Prof Daniel Christ|
|Publisher Name||PROTEIN ENGINEERING DESIGN & SELECTION|
|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|