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

Eric S McLamore, Maria Torres, Justin M Hutchison, Brooke K Mayer, Kaushik Venkiteshwaran

Journal: Current opinion in biotechnology 2024;90():103199

PMID: 39276616

Full Text on Elsevier Science View on PubMed

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.

Address: Department of Civil, Construction and Environmental Engineering, Marquette University, Milwaukee, WI, USA. Electronic address: [email protected].; Department of Civil, Environmental & Architectural Engineering, University of Kansas, Lawrence, KS, USA.; Environmental Engineering and Earth Sciences, Clemson University, Clemson, SC, USA; Agricultural Sciences, Clemson University, Clemson, SC, USA.; Department of Plant and Environmental Sciences, Clemson University, Clemson, SC, USA.; Department of Civil, Coastal and Environmental Engineering, University of South Alabama, Mobile, AL, USA.

DOI: 10.1016/j.copbio.2024.103199

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MeSH Terms: Peptides, Phosphate-Binding Proteins, Phosphates