Journal
PROTEIN ENGINEERING DESIGN & SELECTION
Volume 20, Issue 8, Pages 413-416Publisher
OXFORD UNIV PRESS
DOI: 10.1093/protein/gzm037
Keywords
combinatorial repertoire; molecular evolution; phage display; protein aggregation
Funding
- MRC [MC_U105115240] Funding Source: UKRI
- Medical Research Council [MC_U105115240] Funding Source: researchfish
- Medical Research Council [MC_U105115240] Funding Source: Medline
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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.
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