Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Bellaterra, Barcelona, Spain.
Microb Cell Fact. 2011 Dec 2;10:101. doi: 10.1186/1475-2859-10-101.
Histidine-rich peptides are commonly used in recombinant protein production as purification tags, allowing the one-step affinity separation of the His-tagged proteins from the extracellular media or cell extracts. Genetic engineering makes feasible the post-purification His-tag removal by inserting, between the tag and the main protein body, a target site for trans-acting proteases or a self-proteolytic peptide with regulatable activities. However, for technical ease, His tags are often not removed and the fusion proteins eventually used in this form. In this commentary, we revise the powerful biological properties of histidine-rich peptides as endosomolytic agents and as architectonic tags in nanoparticle formation, for which they are exploited in drug delivery and other nanomedical applications. These activities, generally unknown to biotechnologists, can unwillingly modulate the functionality and biotechnological performance of recombinant proteins in which they remain trivially attached.
组氨酸丰富肽通常被用作重组蛋白生产中的纯化标签，允许一步亲和分离 His 标记的蛋白质与细胞外介质或细胞提取物。基因工程使得通过在标签和主要蛋白质体之间插入靶位点用于反式作用蛋白酶或具有可调节活性的自切割肽，可以在纯化后去除 His 标签成为可能。然而，为了技术上的方便，His 标签通常不被去除，融合蛋白最终以这种形式使用。在这篇评论中，我们回顾了富含组氨酸的肽作为内体溶酶体剂和纳米颗粒形成中的结构标记的强大生物学特性，这些特性在药物输送和其他纳米医学应用中得到了利用。这些活性通常不为生物技术学家所知，但它们可能会在无意中调节其中仍简单附着的重组蛋白的功能和生物技术性能。
