Biological materials possess highly sophisticated material properties that are intrinsically connected to their molecular and intermolecular design. In recent decades, engineers have designed creative synthetic material platforms that translate these properties to tunable material systems in order to address emerging challenges facing society. One intriguing biological property to mimic is the ability of protein to molecularly recognize and bind to specific targets, which could be repurposed to address key challenges such as resource recovery from water or detecting harmful aqueous contaminants. However, tunable bio-inspired material platforms with this function are rare. Here, this thesis presents the design, synthesis, and characterization of a material platform based on peptide amphiphile micelles that exploits the natural binding ability of protein and selectively and reversibly binds to phosphate. By utilizing a stimuli-responsive pH trigger, this material is engineered for resource recovery and detection of phosphate by incorporating a protein-extracted binding sequence into the material framework. In Chapter 2, the prototype design, synthesis, and characterization of single-component peptide amphiphile micelles are described. The fundamental phosphate binding characteristics are probed, including the pH-dependence of binding, selectivity over nitrate and nitrite, and reusability of the material. Molecular dynamics simulations are also employed to gain further insight into the molecular mechanism of binding in this system. Chapter 3 describes an enhanced design based on multi-component peptide amphiphile micelles and single peptide resin systems. This work provides additional insight into design principles for mimicking protein-inspired binding of phosphate in synthetic materials. Chapter 4 describes an unexpected intrinsic fluorescence property that was discovered in these peptide amphiphile micelles according to the aggregation-induced emission (AIE) effect. The fundamental fluorescent properties are characterized, and the ability of this material to signal phosphate binding is described. Chapter 5 summarizes the work and discusses future directions. Overall, this work presents a rational design and thorough study of a novel synthetic material platform that harnesses the targeting ability of proteins, offering valuable insight for future protein-inspired synthetic materials designed to this end.