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Hydrophobic core formation and secondary structure elements in uranyl(vi)-binding peptides†
Koichiro Takao
Physical Chemistry Chemical Physics Pub Date : 01/28/2022 00:00:00 , DOI:10.1039/D1CP05401E
Abstract

Cyclic peptides as well as a modified EF-hand motif of calmodulin have been newly designed to achieve high affinity towards uranyl(VI). Cyclic peptides may be engineered to bind uranyl(VI) to its backbone under acidic conditions, which may enhance its selectivity. For the modified EF-hand motif of calmodulin, strong electrostatic interactions between uranyl(VI) and negatively charged side chains play an important role in achieving high affinity; however, it is also essential to have a secondary structure element and formation of hydrophobic cores in the metal-bound state of the peptide.

Graphical abstract: Hydrophobic core formation and secondary structure elements in uranyl(vi)-binding peptides
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