Tuning peptide self-assembly by an in-tether chiral center

Science Advances
Kuan HuZigang Li

Abstract

The self-assembly of peptides into ordered nanostructures is important for understanding both peptide molecular interactions and nanotechnological applications. However, because of the complexity and various self-assembling pathways of peptide molecules, design of self-assembling helical peptides with high controllability and tunability is challenging. We report a new self-assembling mode that uses in-tether chiral center-induced helical peptides as a platform for tunable peptide self-assembly with good controllability. It was found that self-assembling behavior was governed by in-tether substitutional groups, where chirality determined the formation of helical structures and aromaticity provided the driving force for self-assembly. Both factors were essential for peptide self-assembly to occur. Experiments and theoretical calculations indicate long-range crystal-like packing in the self-assembly, which was stabilized by a synergy of interpeptide π-π and π-sulfur interactions and hydrogen bond networks. In addition, the self-assembled peptide nanomaterials were demonstrated to be promising candidate materials for applications in biocompatible electrochemical supercapacitors.

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Citations

Aug 16, 2019·Chemical Communications : Chem Comm·Kuan HuZigang Li
Jun 29, 2021·Journal of Biomaterials Applications·Lisheng ZhuGang Peng
Jul 10, 2021·Frontiers in Bioengineering and Biotechnology·Yongfang ZhengHu Zhu
Dec 14, 2021·Frontiers in Bioengineering and Biotechnology·Zhen LuoHao Wang

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Methods Mentioned

BETA
circular dichroism
scanning electron microscopy
electron diffraction
x-ray diffraction
transmission electron microscopy
AFM
infrared spectroscopy
Fluorescence
fluorescence spectroscopy
optical microscopy

Software Mentioned

XtalPi
CLEARER
Pro
- Viewer
VASP
NanoScope Analysis

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