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殷黎晨教授课题组与美国伊利诺伊大学香槟分校程建军教授合作课题组在Nature Communications上发表论文
发布时间:2018-03-15 点击:1

题目:

Modulation of Polypeptide Conformation through Donor�Acceptor Transformation of Side-Chain Hydrogen Bonding Ligands

 

作者:

Ziyuan Song1, Rachael A. Mansbach 2, Hua He3, Kuo-Chih Shih4,5, Ryan Baumgartner6, Nan Zheng1, Xiaochu Ba6, Yinzhao Huang6, Deepak Mani1, Yun Liu7,8, Yao Lin 4,9, Mu-Ping Nieh4,10, Andrew L. Ferguson 1,11,*, Lichen Yin3,* & Jianjun Cheng1,*

 

单位:

1 Department of Materials Science and Engineering, University of Illinois at Urbana�Champaign, Urbana, Illinois 61801, USA.

2Department of Physics, University of Illinois at Urbana�Champaign, Urbana, Illinois 61801, USA.

3Jiangsu Key Laboratory for Carbon-Based Functional Materials & Devices, Institute of Functional Nano & Soft Materials (FUNSOM), Soochow University, Suzhou 215123, China.

4Polymer Program, Institute of Materials Science, University of Connecticut, Storrs, Connecticut 06269, USA.

5Department of Agricultural Chemistry, National Taiwan University, Taipei 10617, Taiwan.

6Department of Chemistry, University of Illinois at Urbana�Champaign, Urbana, Illinois 61801, USA.

7Center for Neutron Research, National Institute of Standards and

Technology, Gaithersburg, Maryland 20899, USA.

8Department of Chemical and Biomolecular Engineering, University of Delaware, Newark 19716, USA.

9Department of Chemistry, University of Connecticut, Storrs, Connecticut 06269, USA.

10Department of Chemical and Biomolecular Engineering, University of Connecticut, Storrs, Connecticut 06269, USA.

11Department of Chemical and Biomolecular Engineering, University of Illinois at Urbana�Champaign, Urbana, Illinois 61801, USA.

 

摘要:

Synthetic polypeptides have received increasing attention due to their ability to form higher ordered structures similar to proteins. The control over their secondary structures, which enables dynamic conformational changes, is primarily accomplished by tuning the side-chain hydrophobic or ionic interactions. Herein we report a strategy to modulate the conformation of polypeptides utilizing donor�acceptor interactions emanating from side-chain H-bonding ligands. Specifically, 1,2,3-triazole groups, when incorporated onto polypeptide side-chains, serve as both H-bond donors and acceptors at neutral pH and disrupt the α-helical conformation. When protonated, the resulting 1,2,3-triazolium ions lose the ability to act as H-bond acceptors, and the polypeptides regain their α-helical structure. The conformational change of triazole polypeptides in response to the donor-acceptor pattern was conclusively demonstrated using both experimental-based and simulation-based methods. We further showed the utility of this transition by designing smart, cell-penetrating polymers that undergo acid-activated endosomal escape in living cells.

 

影响因子:

12.124

 

分区情况:

一区

 

链接:

https://www.nature.com/articles/s41467-017-00079-5

 

责任编辑:向丹婷


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