Chiral Recognition of Self-Assembled Peptides on MoS<sub>2</sub> via Lattice Matching
Chiral Recognition of Self-Assembled Peptides on MoS<sub>2</sub> via Lattice Matching
复制标题
通过晶格匹配对 MoS<sub>2</sub> 上自组装肽进行手性识别
DOI：
10.1021/acs.langmuir.1c00792
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发表时间：
2021
期刊：
影响因子：
3.9
通讯作者：
Hayamizu Yuhei
中科院分区：
文献类型：
--
作者：
Sun Linhao;Li Peiying;Seki Takakazu;Tsuchiya Shohei;Yatsu Kazuki;Narimatsu Takuma;Sarikaya Mehmet;Hayamizu Yuhei
研究了多肽在固体表面的手性识别，以便更好地了解其在立体化学和对映选择性催化中的应用。然而，从小肽（如二肽）开始，了解大生物分子（如寡肽或具有较大序列的肽）的手性识别是具有挑战性的。此外，它们在液体条件下进行手性识别的内在机制的实验研究很少。本研究利用超原位原子力显微镜（AFM）研究了l/d型多肽自组装结构在二硫化钼（MoS2）上的手性识别。我们选择了三角形的单层二硫化钼作为多肽自组装的底物。利用二硫化钼的小面边缘作为标记来识别其有序结构的晶体取向。我们发现两种肽对映体在MoS2上形成纳米线，根据MoS2的facet边缘具有镜像对称。从原位AFM测量中，我们发现了自组装结构中单个细胞的尺寸，并提出了肽与mos2晶格之间的晶格匹配模型。通过将多肽序列和表面晶格从二硫化钼转变为石墨，进一步研究了手性识别的晶格匹配。这项工作进一步加深了对生物分子手性识别的理解，并将引导我们在未来合理设计具有预期功能的肽手性自组装结构的特定形态和构象。
Chiral recognition of peptides on solid surfaces has been studied for a better understanding of their assembly mechanism toward its applications in stereochemistry and enantioselective catalysis. However, moving from small peptides such as dipeptides, understanding the chiral recognition of larger biomolecules such as oligopeptides or peptides with a larger sequence is challenging. Furthermore, their intrinsic mechanism for chiral recognition in liquid conditions was poorly investigated experimentally. Here, we used in/ex situ atomic force microscopy (AFM) to investigate the chiral recognition of self-assembled structures ofl/d-type peptides on molybdenum disulfide (MoS2). We chose single-layer MoS2with a triangular shape as a substrate for the self-assembly of peptides. The facet edges of MoS2were utilized as a landmark to identify the crystallographic orientation of their ordered structures. We found both peptide enantiomers formed nanowires on MoS2with a mirror symmetry according to the facet edges of MoS2. From in situ AFM measurements, we found a dimension of a unit cell in the self-assembled structure and proposed a model of lattice matching between peptides and MoS2lattice. The lattice matching for chiral recognition was further investigated by changing peptide sequences and surface lattice from MoS2to graphite. This work further deepened the understanding of biomolecular chiral recognition and will lead us to rationally design specific morphologies and conformations of chiral self-assembled structures of peptides with expected functions in the future.