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.
This paper introduces a modi ed TLS-Prony method which uses data decimation. The use of data decimation results in the reduction in the computational complexity in a variety of applications by allowing several low order estimations to be performed rather than one high order estimation. We also present an analysis of pole variance statistics for the modi ed TLS-Prony method which is used to explain and quantify the characteristics of decimation. We show that using decimation we can obtain comparable performance results at a fraction of the computational cost.
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.
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