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Review
. 2024 Dec:90:103199.
doi: 10.1016/j.copbio.2024.103199. Epub 2024 Sep 13.

Phosphate-binding proteins and peptides: from molecular mechanisms to potential applications

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Review

Phosphate-binding proteins and peptides: from molecular mechanisms to potential applications

Brooke K Mayer et al. Curr Opin Biotechnol. 2024 Dec.

Abstract

Selective binding of phosphate is vital to multiple aims including phosphate transport into cells and phosphate-targeted applications such as adsorption-based water treatment and sensing. High-affinity phosphate-binding proteins and peptides offer a nature-inspired means of efficiently binding and separating phosphate from complex matrices. The binding protein PstS is characterized by a Venus flytrap topology that confers exceptional phosphate affinity and selectivity, and is effective even at low phosphate concentrations, all of which are essential for applications such as phosphate sensing, removal, and recovery. The binding event is reversible under controlled conditions, making it germane to catch-and-release objectives that advance phosphorus sustainability. Peptides such as the P loop motif are also promising for such applications. Future advances in protein/peptide design can contribute to increased implementation in engineered systems.

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Conflict of interest statement

Declaration of Competing Interest The authors declare the following financial interests/personal relationships which may be considered as potential competing interests: B.K. Mayer and K. Venkiteshwaran are co-inventors on a patent application entitled “Process for controlled adsorption and desorption of phosphate from liquids using phosphate-selective proteins”. The authors declare no other potential conflicts of interest.

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