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With plenty of charges and rich functional groups, bovine serum albumin (BSA) protein provides effective transport for multiple metallic ions inside blood vessels. Inspired by the unique ionic transport function, we develop a BSA protein coating to stabilize Li anode, regulate Li+ transport, and resolve the Li dendrite growth for Li metal batteries (LMBs). The experimental and simulation studies demonstrate that the coating has strong interactions with Li metal, increases the wetting with electrolyte, reduces the electrolyte/Li side reactions, and significantly suppresses the Li dendrite formation. As a result, the BSA coating exhibits excellent stability in the electrolyte and improves the performance of Li|Cu and Li|Li cells as well as the LiFePO4|Li batteries. This work reveals that LMBs can benefit from the biological function of BSA, i.e., special transport capability of metallic ions, and lays an important foundation in design of protein-based materials for effectively enhancing the electrochemical performance of energy storage systems. 

Suffering from critical instability of lithium (Li) anode, the most commercial electrolytes, carbonate-ester electrolytes, have been restrictedly used in high-energy Li metal batteries (LMBs) despite of their broad implementation in lithium-ion batteries. Here, abundant, natural corn protein, zein, is exploited as a novel additive to stabilize Li anode and effectively prolong the cycling life of LMBs based on carbonate-ester electrolyte. It is discovered that the denatured zein is involved in the formation of solid electrolyte interphase (SEI), guides Li+ deposition and repairs the cracked SEI. In specific, the zein-rich SEI benefits the anion immobilization, enabling uniform Li+ deposition to diminish dendrite growth; the preferential zein-Li reaction effectively repairs the cracked SEI, protecting Li from parasite reactions. The resulting symmetrical Li cell exhibits a prolonged cycling life to over 350 h from <200 h for pristine cell at 1 mA cm􀀀 2 with a capacity of 1 mAh cm^ 2. Paired with LiFePO4 cathode, zein additive markedly improves the electrochemical performance including a higher capacity of 130.1 mAh g^ 1 and a higher capacity retention of ~ 80 % after 200 cycles at 1 C. This study demonstrates a natural protein to be an effective additive for the most commercial electrolytes for advancing performance of LMBs. 

Low ionic conductivity is one of the main hurdles for the practical application of advanced all‐solid‐state lithium‐ion batteries. Protein‐based solid electrolytes are recently proposed and can potentially provide both high ionic conductivity and high mechanical properties due to the decoupled ion transport mechanism. In this work, the effects of lithium salts and protein structures on the performance of protein‐based electrolytes through both ab initio density functional theory calculations and experiments are systematically investigated. The results show that the anions can be strongly locked by the charged amino acids, thus providing intermediate hopping sites for lithium‐ion, reducing energy barrier for lithium‐ion transport, and then enhancing the ionic conductivity. These calculations also demonstrate that need to be locked at appropriate positions by properly controlling the protein structures in order to provide bridging effects and facilitate lithium‐ion transport. The findings are consistent with the experimental observations and can provide guidance for design and optimization of protein‐based solid electrolytes.

 

Decoupling the ion motion and segmental relaxation is significant for developing advanced solid polymer electrolytes with high ionic conductivity and high mechanical properties. Our previous work proposed a decoupled ion transport in a novel protein-based solid electrolyte. Herein, we investigate the detailed ion interaction/transport mechanisms through first-principles density functional theory (DFT) calculations in a vacuum space. Specifically, we study the important roles of charged amino acids from proteins. Our results show that the charged amino acids (i.e., Arg and Lys) can strongly lock anions (ClO4−). When locked at a proper position (determined from the molecular structure of amino acids), the anions can provide additional hopping sites and facilitate Li+ transport. The findings are supported from our experiments of two protein solid electrolytes, in which the soy protein (with plenty of charged amino acids) electrolyte shows much higher ionic conductivity and lower activation energy in comparison to the zein (lack of charged amino acids) electrolyte.