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Updated: Jun 13, 2025

Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy
Published on: March 6, 2017
Phosphate-binding proteins and peptides: from molecular mechanisms to potential applications
Brooke K Mayer1, Justin M Hutchison2, Eric S McLamore3
1Department of Civil, Construction and Environmental Engineering, Marquette University, Milwaukee, WI, USA.
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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