Zhao-Jun Yan

Fudan University

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Jun‐Li Hou

Fudan University

Lehui Xiao

Central South University

Zhan‐Ting Li

Fudan University

Zhongju Ye

Zhengzhou University

Wenning Wang

Fudan University

Chaoqing Dong

Shanghai Jiao Tong University

Maohua Yang

SP Technology (South Korea)

Yunfeng Wang

Eye & ENT Hospital of Fudan University

Yonghong Fu

Xi'an University of Architecture and Technology

Yawei Li

Shandong Agricultural University

Cooperative Institutions

Fudan University

Collaborative Innovation Center of Chemistry for Energy Materials

Shanghai Jiao Tong University

Chinese Academy of Sciences

Nankai University

Sichuan University

Zhejiang University

Metal Matrix Cast Composites (United States)

State Key Laboratory of Metal Matrix Composites

State Council of the People's Republic of China

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Voltage-Driven Flipping of Zwitterionic Artificial Channels in Lipid Bilayers to Rectify Ion Transport

Journal of the American Chemical Society (2021)

Zhao-Jun Yan Yawei Li Maohua Yang Yonghong Fu Rongrong Wen

We developed a voltage-sensitive artificial transmembrane channel by mimicking the dipolar structure of natural alamethicin channel. The artificial channel featured a zwitterionic structure and could undergo voltage-driven flipping in the lipid bilayers. Importantly, this flipping of the channel could lead to their directional alignment in the bilayers and rectifying behavior for ion transport.

Alamethicin

Transmembrane channels

10.1021/jacs.1c06000

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Citations (34)

Charged Tubular Supramolecule Boosting Multivalent Interactions for the Drastic Suppression of Aβ Fibrillation

Nano Letters (2021)

Zhongju Ye Zhao-Jun Yan Chenhong Zhang Jun‐Li Hou Shijing Yue

Anti-Aβ therapy has dominated clinical trials for the prevention and treatment of Alzheimer's disease (AD). However, suppressing Aβ aggregation and disintegrating mature fibrils simultaneously remains a great challenge. In this work, we developed a new strategy using a charged tubular supramolecule (CTS) with pillar[5]arene as the backbone and modifying amino and carboxyl groups at the tubular terminals (noted as CTS-A, CTS-A/C, and CTS-C, respectively) to suppress Aβ fibrillation for the first time. According to the spectroscopic and microscopic characterizations, Aβ40 fibrillation can be efficiently suppressed by CTS-A in a very low inhibitor:peptide (I:P) molar ratio (1:10). A greatly alleviated cytotoxic effect of Aβ peptides after the inhibition or disaggregation process is further disclosed. The well-organized supramolecular structure drives multivalent interaction and gains enhanced efficiency on amyloid fibrillar modulation. These results open a new path for the design of supramolecules in the application of AD treatment.

Fibrillation

Molar ratio

Pillar

10.1021/acs.nanolett.1c04007

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Artificial Aquaporin That Restores Wound Healing of Impaired Cells

Journal of the American Chemical Society (2020)

Zhao-Jun Yan Dongdong Wang Zhongju Ye Ting Fan Gang Wu

Artificial aquaporins are synthetic molecules that mimic the structure and function of natural aquaporins (AQPs) in cell membranes. The development of artificial aquaporins would provide an alternative strategy for treatment of AQP-related diseases. In this report, an artificial aquaporin has been constructed from an amino-terminated tubular molecule, which operates in a unimolecular mechanism. The artificial channel can work in cell membranes with high water permeability and selectivity rivaling those of AQPs. Importantly, the channel can restore wound healing of the cells that contain function-lost AQPs.

Cell permeability

Aquaporin 1

Cell membrane

Water Transport

Membrane permeability

10.1021/jacs.0c00601

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Citations (71)