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M13 噬菌体主要外壳蛋白突变以增加与外源化合物的缀合。

Mutation of M13 Bacteriophage Major Coat Protein for Increased Conjugation to Exogenous Compounds.

机构信息

School of Biosciences , University of Birmingham , Edgbaston, Birmingham , West Midlands , B15 2TT , United Kingdom.

出版信息

Bioconjug Chem. 2018 Jun 20;29(6):1872-1875. doi: 10.1021/acs.bioconjchem.8b00307. Epub 2018 Jun 1.

Abstract

Over the past ten years there has been increasing interest in the conjugation of exogenous compounds to the surface of the M13 bacteriophage. M13 offers a convenient scaffold for the development of nanoassemblies with useful functions, such as highly specific drug delivery and pathogen detection. However, the progress of these technologies has been hindered by the limited efficiency of conjugation to the bacteriophage. Here we generate a mutant version of M13 with an additional lysine residue expressed on the outer surface of the M13 major coat protein, pVIII. We show that this mutation is accommodated by the bacteriophage and that up to an additional 520 exogenous groups can be attached to the bacteriophage surface via amine-directed conjugation. These results could aid the development of high payload drug delivery nanoassemblies and pathogen detection systems with increased sensitivity.

摘要

在过去的十年中,人们对将外源化合物缀合到 M13 噬菌体表面越来越感兴趣。M13 为开发具有有用功能的纳米组装体提供了一个方便的支架,例如高度特异性的药物输送和病原体检测。然而,这些技术的进展受到噬菌体缀合效率有限的阻碍。在这里,我们生成了一种突变体版本的 M13,在 M13 主要外壳蛋白 pVIII 的外表面表达额外的赖氨酸残基。我们表明,这种突变被噬菌体所容纳,并且通过胺定向缀合可以将多达另外 520 个外源基团附着到噬菌体表面。这些结果可能有助于开发具有更高敏感性的高载药药物输送纳米组装体和病原体检测系统。

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