TY - JOUR A1 - Xu, Yaolin A1 - Dong, Kang A1 - Jie, Yulin A1 - Adelhelm, Philipp A1 - Chen, Yawei A1 - Xu, Liang A1 - Yu, Peiping A1 - Kim, Junghwa A1 - Kochovski, Zdravko A1 - Yu, Zhilong A1 - Li, Wanxia A1 - LeBeau, James A1 - Shao-Horn, Yang A1 - Cao, Ruiguo A1 - Jiao, Shuhong A1 - Cheng, Tao A1 - Manke, Ingo A1 - Lu, Yan T1 - Promoting mechanistic understanding of lithium deposition and solid-electrolyte interphase (SEI) formation using advanced characterization and simulation methods: recent progress, limitations, and future perspectives JF - Avanced energy materials N2 - In recent years, due to its great promise in boosting the energy density of lithium batteries for future energy storage, research on the Li metal anode, as an alternative to the graphite anode in Li-ion batteries, has gained significant momentum. However, the practical use of Li metal anodes has been plagued by unstable Li (re)deposition and poor cyclability. Although tremendous efforts have been devoted to the stabilization of Li metal anodes, the mechanisms of electrochemical (re-)deposition/dissolution of Li and solid-electrolyte-interphase (SEI) formation remain elusive. This article highlights the recent mechanistic understandings and observations of Li deposition/dissolution and SEI formation achieved from advanced characterization techniques and simulation methods, and discusses major limitations and open questions in these processes. In particular, the authors provide their perspectives on advanced and emerging/potential methods for obtaining new insights into these questions. In addition, they give an outlook into cutting-edge interdisciplinary research topics for Li metal anodes. It pushes beyond the current knowledge and is expected to accelerate development toward a more in-depth and comprehensive understanding, in order to guide future research on Li metal anodes toward practical application. KW - advanced characterization KW - Li deposition KW - Li dissolution KW - Li metal KW - anodes KW - mechanistic understanding KW - solid-electrolyte-interphase KW - theoretical simulation Y1 - 2022 U6 - https://doi.org/10.1002/aenm.202200398 SN - 1614-6832 SN - 1614-6840 VL - 12 IS - 19 PB - Wiley CY - Weinheim ER - TY - JOUR A1 - Kang, Yu A1 - Gohlke, Ulrich A1 - Engström, Olof A1 - Hamark, Christoffer A1 - Scheidt, Tom A1 - Kunstmann, Ruth Sonja A1 - Heinemann, Udo A1 - Widmalm, Göran A1 - Santer, Mark A1 - Barbirz, Stefanie T1 - Bacteriophage Tailspikes and Bacterial O-Antigens as a Model System to Study Weak-Affinity Protein-Polysaccharide Interactions JF - Journal of the American Chemical Society N2 - Understanding interactions of bacterial surface polysaccharides with receptor protein scaffolds is important for the development of antibiotic therapies. The corresponding protein recognition domains frequently form low-affinity complexes with polysaccharides that are difficult to address with experimental techniques due to the conformational flexibility of the polysaccharide. In this work, we studied the tailspike protein (TSP) of the bacteriophage Sf6. Sf6TSP binds and hydrolyzes the high-rhamnose, serotype Y O-antigen polysaccharide of the Gram-negative bacterium Shigella flexneri (S. flexneri) as a first step of bacteriophage infection. Spectroscopic analyses and enzymatic cleavage assays confirmed that Sf6TSP binds long stretches of this polysaccharide. Crystal structure analysis and saturation transfer difference (STD) NMR spectroscopy using an enhanced method to interpret the data permitted the detailed description of affinity contributions and flexibility in an Sf6TSP-octasaccharide complex. Dodecasaccharide fragments corresponding to three repeating units of the O-antigen in complex with Sf6TSP were studied computationally by molecular dynamics simulations. They showed that distortion away from the low-energy solution conformation found in the octasaccharide complex is necessary for ligand binding. This is in agreement with a weak-affinity functional polysaccharide protein contact that facilitates correct placement and thus hydrolysis of the polysaccharide close to the catalytic residues. Our simulations stress that the flexibility of glycan epitopes together with a small number of specific protein contacts provide the driving force for Sf6TSP-polysaccharide complex formation in an overall weak-affinity interaction system. Y1 - 2016 U6 - https://doi.org/10.1021/jacs.6b00240 SN - 0002-7863 VL - 138 SP - 9109 EP - 9118 PB - American Chemical Society CY - Washington ER - TY - CHAP A1 - Kang, Yu A1 - Barbirz, Stefanie A1 - Gohlke, Ulrich A1 - Santer, Mark T1 - Molecular dynamics study on the interaction of O-antigen polysaccharides of the gram-negative bacterium Shigella flexneri with the tail-spike-protein of bacteriophage Sf6 T2 - Abstracts of papers : joint conference / The Chemical Institute of Cananda, CIC, American Chemical Society, ACS Y1 - 2014 SN - 0065-7727 VL - 248 PB - American Chemical Society CY - Washington ER - TY - JOUR A1 - Kang, Yu A1 - Barbirz, Stefanie A1 - Lipowsky, Reinhard A1 - Santer, Mark T1 - Conformational Diversity of O-Antigen Polysaccharides of the Gram-Negative Bacterium Shigella flexneri Serotype Y JF - The journal of physical chemistry : B, Condensed matter, materials, surfaces, interfaces & biophysical chemistry Y1 - 2014 U6 - https://doi.org/10.1021/jp4111713 SN - 1520-6106 VL - 118 IS - 9 SP - 2523 EP - 2534 PB - American Chemical Society CY - Washington ER -