Novel Cyclopeptide Bolaamphiphile for Constructing Supramolecular Nanotubes  

Novel Cyclopeptide Bolaamphiphile for Constructing Supramolecular Nanotubes

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作  者:Siyong Qin Qingrong Wang Yi Pei Mengyun Peng Renxi Zhuo Xianzheng Zhang 

机构地区:Key Laboratory of Biomedical Polymers of Ministry of Education & Department of Chemistry, Wuhan University, Wuhan, Hubei 430072, China Email: Xianzheng Zhang (xz-zhang@whu.edu.cn)[*]Key Laboratory of Biomedical Polymers of Ministry of Education & Department of Chemistry, Wuhan University, Wuhan, Hubei 430072, China

出  处:《Chinese Journal of Chemistry》2014年第1期22-26,共5页中国化学(英文版)

摘  要:A novel dicyclopeptide-based bolaamphiphile was synthesized.The hydrophilic cyclopeptide fragments were linked to an alkyl chain 1,6-bis(maleimido)hexane,which acted as a hydrophobic spacer.The transmission electron microscopy (TEM) observation indicated that the cyclopeptide bolaamphiphile (CPB) self-assembled into the nanotubes with a thickness of about 3 nm.Based on the optimized molecular conformation obtained via MM2 method,the length of CPB was demonstrated to be around 4 nm,implying that the nanotubes were single-walled.Fourier transform infrared spectroscopy (FT-IR) and circular dichroism (CD) analysis showed that the cyclopeptides in CPB mainly acted as the hydrophilic headgroups,rather than providing the well-ordered hydrogen bonding interaction responsible for β-sheet conformation.To investigate the special self-assembly behavior of CPB,the single cyclopeptide (CP) without the connection of the linker was synthesized.Further investigation indicated that the CP molecules can not form tubular structures but nanofibers.A novel dicyclopeptide-based bolaamphiphile was synthesized.The hydrophilic cyclopeptide fragments were linked to an alkyl chain 1,6-bis(maleimido)hexane,which acted as a hydrophobic spacer.The transmission electron microscopy (TEM) observation indicated that the cyclopeptide bolaamphiphile (CPB) self-assembled into the nanotubes with a thickness of about 3 nm.Based on the optimized molecular conformation obtained via MM2 method,the length of CPB was demonstrated to be around 4 nm,implying that the nanotubes were single-walled.Fourier transform infrared spectroscopy (FT-IR) and circular dichroism (CD) analysis showed that the cyclopeptides in CPB mainly acted as the hydrophilic headgroups,rather than providing the well-ordered hydrogen bonding interaction responsible for β-sheet conformation.To investigate the special self-assembly behavior of CPB,the single cyclopeptide (CP) without the connection of the linker was synthesized.Further investigation indicated that the CP molecules can not form tubular structures but nanofibers.

关 键 词:CYCLOPEPTIDE BOLAAMPHIPHILE self-assembly NANOTUBE 

分 类 号:O6[理学—化学]

 

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