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荧光相关光谱分析分子拥挤效应对β-环糊精肽自组装成人工病毒衣壳的影响。

Fluorescence Correlation Spectroscopy Analysis of Effect of Molecular Crowding on Self-Assembly of -Annulus Peptide into Artificial Viral Capsid.

机构信息

Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, Tottori 680-8552, Japan.

Centre for Research on Green Sustainable Chemistry, Tottori University, Tottori 680-8552, Japan.

出版信息

Int J Mol Sci. 2021 Apr 30;22(9):4754. doi: 10.3390/ijms22094754.

DOI:10.3390/ijms22094754
PMID:33946174
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8125178/
Abstract

Recent progress in the design of self-assembling peptides has enabled the construction of peptide-based viral capsids. Previously, we demonstrated that 24-mer -annulus peptides from tomato bushy stunt virus spontaneously self-assemble into an artificial viral capsid. Here we propose to use the artificial viral capsid through the self-assembly of -annulus peptide as a simple model to analyze the effect of molecular crowding environment on the formation process of viral capsid. Artificial viral capsids formed by co-assembly of fluorescent-labelled and unmodified -annulus peptides in dilute aqueous solutions and under molecular crowding conditions were analyzed using fluorescence correlation spectroscopy (FCS). The apparent particle size and the dissociation constant ( of the assemblies decreased with increasing concentration of the molecular crowding agent, i.e., polyethylene glycol (PEG). This is the first successful in situ analysis of self-assembling process of artificial viral capsid under molecular crowding conditions.

摘要

最近在自组装肽设计方面的进展使得基于肽的病毒衣壳的构建成为可能。以前,我们证明了来自番茄丛矮病毒的 24 个氨基酸 - 环肽可以自发组装成人工病毒衣壳。在这里,我们建议使用人工病毒衣壳,通过 - 环肽的自组装作为一个简单的模型来分析分子拥挤环境对病毒衣壳形成过程的影响。在稀释水溶液中和分子拥挤条件下,通过荧光标记和未修饰的 - 环肽共组装形成的人工病毒衣壳使用荧光相关光谱法(FCS)进行分析。随着分子拥挤试剂,即聚乙二醇(PEG)浓度的增加,组装体的表观粒径和离解常数(Kd)降低。这是首次在分子拥挤条件下成功地对人工病毒衣壳的自组装过程进行原位分析。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/942a/8125178/6e190d75b0a5/ijms-22-04754-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/942a/8125178/c10457a88d26/ijms-22-04754-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/942a/8125178/21551f66e0fc/ijms-22-04754-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/942a/8125178/53d1ad8698e8/ijms-22-04754-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/942a/8125178/6a67c6dc3ea8/ijms-22-04754-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/942a/8125178/6e190d75b0a5/ijms-22-04754-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/942a/8125178/c10457a88d26/ijms-22-04754-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/942a/8125178/21551f66e0fc/ijms-22-04754-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/942a/8125178/53d1ad8698e8/ijms-22-04754-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/942a/8125178/6a67c6dc3ea8/ijms-22-04754-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/942a/8125178/6e190d75b0a5/ijms-22-04754-g005.jpg

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