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- W1985061567 abstract "Chicken avidin is a key component used in a wide variety of biotechnological applications. Here we present a circularly permuted avidin (cpAvd4→3) that lacks the loop between β-strands 3 and 4. Importantly, the deletion of the loop has a positive effect on the binding of 4′-hydroxyazobenzene-2-carboxylic acid (HABA) to avidin. To increase the HABA affinity of cpAvd4→3 even further, we mutated asparagine 118 on the bottom of the ligand-binding pocket to methionine, which simultaneously caused a significant drop in biotin-binding affinity. The X-ray structure of cpAvd4→ 3(N118M) allows an understanding of the effect of mutation to biotin-binding, whereas isothermal titration calorimetry revealed that the relative binding affinity of biotin and HABA had changed by over one billion-fold between wild-type avidin and cpAvd4→3(N118M). To demonstrate the versatility of the cpAvd4→3 construct, we have shown that it is possible to link cpAvd4→3 and cpAvd5→4 to form the dual-chain avidin called dcAvd2. These novel avidins might serve as a basis for the further development of self-organising nanoscale avidin building blocks." @default.
- W1985061567 created "2016-06-24" @default.
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- W1985061567 date "2008-05-05" @default.
- W1985061567 modified "2023-10-10" @default.
- W1985061567 title "Rational Modification of Ligand-Binding Preference of Avidin by Circular Permutation and Mutagenesis" @default.
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- W1985061567 doi "https://doi.org/10.1002/cbic.200700671" @default.
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