Searching for highly selective, efficient, and low-toxicity chelating agents is central to resolving uranium contamination in vivo. Peptides composed of amino acids exhibit very low toxicity for accumulation in the human body and have been proven effective in chelating actinides within the human body. Herein, we report a rationally designed short phosphorylated peptide sequence PP-B, which exhibits high affinity and selectivity for uranyl compared to other trace elements present in the body (such as Na+, K+, Ca2+, Co2+, Fe2+, Fe3+, Mg2+, Mn2+, Zn2+). The association constant for the peptide–uranyl complex is calculated to be 7.3 ×105 M−1. The result of DFT calculation shows that the phosphate group binds strongly to the UO22+ center, potentially accounting for the peptide's strong affinity towards UO22+. The results of in vivo uranyl decorporation assays reveal that PP-B has a much lower toxicity and a much higher decorporation efficiency than that of the clinically approved DTPA. These findings render PP-B a promising candidate for utilization as a novel decorporation agent.
A low-toxicity uranyl-selective-binding linear pentapeptide sequence as a potential uranium decorporation agent
Xiaohong Tan,Libing Yu,Xindan Liao,Chun Chen,Jian Chu,Zhonghua Xiong,B.Y. Xia,Wei‐Ying Tang,Xijian Li,Yanyan Liu
Published 2024 in RSC Advances
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- Publication year
2024
- Venue
RSC Advances
- Publication date
2024-12-10
- Fields of study
Medicine, Chemistry, Environmental Science
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Semantic Scholar, PubMed
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