LAUSR

Biotemplating presents a promising approach to improve the performance of inorganic materials via specific control over morphology, crystal structure, and the size of particles during synthesis and assembly. Among other biotemplates, solid binding polypeptides (SBPs) isolated for the material of interest provide high binding affinity and selectivity due to distinct combinations of functional groups found in amino acids. Nanomaterials assembled and synthesized with SBPs have found widespread applications from drug delivery to catalysis and energy storage due to their improved properties. In this study, the authors describe the identification of SBPs for binding to Li-ion battery cathode materials LiCoPO4, LiMn1.5Ni0.5O4, and LiMn2O4, which all have potential for improvement toward their theoretical values. The binding affinity of isolated peptides was assessed via phage binding assays and confirmed with electron microscopy in order to select for potential biotemplates. The authors demonstrate ten binding peptides for each material and analyze the sequences for enrichment in specific amino acids toward each structure (olivine and spinel oxide), as well as the test for specificity of selected sequences. In further studies, the authors believe that the isolated SBPs will serve as a template for synthesis and aid in assembly of cathode materials resulting in improved electrochemical properties for Li-ion batteries.