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A Comparative Study on the Self-Assembly of Peptide TGV-9 by In Situ Atomic Force Microscopy

Published online by Cambridge University Press:  13 February 2020

Yaping Li ,
Na Li ,
Lei Wang ,
Qinhua Lu ,
Xiang Ji  and
Feng Zhang Open the ORCID record for Feng Zhang [Opens in a new window]
Yaping Li
Affiliation:
School of Life Science and Technology, Inner Mongolia University of Science and Technology, Baotou014010, P. R. China
Na Li
Affiliation:
Terahertz Technology Innovation Research Institute, Shanghai Key Laboratory of Modern Optical System, Terahertz Science Cooperative Innovation Center, University of Shanghai for Science and Technology, 516 Jungong Road, Shanghai200093, P. R. China Biomedical Nanocenter, School of Life Science, Inner Mongolia Agricultural University, Hohhot010018, P. R. China
Lei Wang
Affiliation:
School of Life Science and Technology, Inner Mongolia University of Science and Technology, Baotou014010, P. R. China
Qinhua Lu
Affiliation:
School of Life Science and Technology, Inner Mongolia University of Science and Technology, Baotou014010, P. R. China
Xiang Ji*
Affiliation:
School of Life Science and Technology, Inner Mongolia University of Science and Technology, Baotou014010, P. R. China
Feng Zhang*
Affiliation:
School of Life Science and Technology, Inner Mongolia University of Science and Technology, Baotou014010, P. R. China Biomedical Nanocenter, School of Life Science, Inner Mongolia Agricultural University, Hohhot010018, P. R. China Key Laboratory of Oral Medicine, Department of Biomedical Engineering, School of Basic Medical Sciences, Guangzhou Institute of Oral Disease, Stomatology Hospital, Guangzhou Medical University, Guangzhou511436, P. R. China
*
*Authors for correspondence: Xiang Ji, E-mail: jixiang@imust.cn; Feng Zhang, E-mail: fengzhang1978@hotmail.com
*Authors for correspondence: Xiang Ji, E-mail: jixiang@imust.cn; Feng Zhang, E-mail: fengzhang1978@hotmail.com
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Abstract

Previous studies of amyloid diseases reported that the aggregating proteins share a similar conserved peptide sequence which can form the cross-β-sheet-containing nanostructures like nanofilaments. The template-assisted self-assembly (TASA) of peptides on inorganic substrates with different hydrophilicity could be an alternative approach to shed light on the fibrillization mechanism of proteins/peptides in vivo. To figure out the effect of interfaces on amyloid aggregation, we herein employed in situ atomic force microscopy (AFM) to investigate the self-assembling of a Parkinson disease-related core peptide sequence (TGV-9) on a hydrophobic liquid–solid interface via real-time observation of the dynamic fibrillization process. The results show that TGV-9 forms one-dimensional nanostructures on the surface of highly ordered pyrolytic graphite (HOPG) with three preferred growth orientations, which are consistent with the atomic lattice of HOPG, indicating an epitaxial growth or TASA. Conversely, the nanostructures formed in bulk solution can be free-standing nanofilaments, and the fibrillization mechanism is different from that on HOPG. These results could not only deepen the understanding of the protein/peptide aggregation mechanism but also benefit for the early diagnosis and clinic treatment of related diseases.

Keywords

in situ atomic force microscopynanofilamenttemplate-assisted self-assemblyTGV-9α-synuclein
Type
Biological Applications
Information
Microscopy and Microanalysis , Volume 26 , Issue 2 , April 2020 , pp. 319 - 325
Copyright
Copyright © Microscopy Society of America 2020

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