期刊
PROTEIN ENGINEERING DESIGN & SELECTION
卷 20, 期 8, 页码 413-416出版社
OXFORD UNIV PRESS
DOI: 10.1093/protein/gzm037
关键词
combinatorial repertoire; molecular evolution; phage display; protein aggregation
资金
- MRC [MC_U105115240] Funding Source: UKRI
- Medical Research Council [MC_U105115240] Funding Source: researchfish
- Medical Research Council [MC_U105115240] Funding Source: Medline
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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