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Reversible loading of thiol-modified curcumin in an engineered protein capsid

机译：工程蛋白衣壳中可逆负载的巯基修饰姜黄素

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The dodecahedral capsid formed by Aquifex aeolicus lumazine synthase (AaLS) is a promising protein scaffold for bionanotechnological applications. A cysteine was installed at the inner surface of the AaLS capsid to give a variant (AaLS-IC) that can covalently capture small-molecule thiols in its hollow interior. Cargo loading utilizes a two-stage thiol–disulfide exchange process, involving the initial formation of an activated disulfide adduct between AaLS-IC and 2-nitro-5-thiobenzoate (NTB) followed by displacement of the NTB by an incoming guest molecule. Using a thiol-containing curcumin derivative (cur-SH) as a model guest, we show that about 41 guest molecules can be loaded per capsid. The sequestration of cur-SH inside the capsid increases its solubility in aqueous buffer by more than 30-fold. Further, the guest can be released upon treatment with tris(2-carboxyethyl)phosphine, which reduces the disulfide bond tethering cur-SH to the capsid. Thus, the AaLS-IC capsid can act as a container for small-molecule thiols, and guest release can be triggered by reducing agents.
机译：由 Aquifex aeolicus lumazine合酶（AaLS）形成的十二面体衣壳是用于生物技术应用的有前途的蛋白质支架。将半胱氨酸安装在AaLS衣壳的内表面，以产生一种变体（AaLS-IC），该变体可以共价捕获其空心内部的小分子硫醇。货物装载采用两阶段的巯基-二硫键交换过程，包括在AaLS-IC和2-硝基-5-硫代苯甲酸酯（NTB）之间最初形成活化的二硫加合物，然后由传入的客体分子取代NTB。使用含硫醇的姜黄素衍生物（cur-SH）作为模型来宾，我们显示每个衣壳可以装载约41个来宾分子。衣壳内部的cur-SH螯合将其在水性缓冲液中的溶解度提高了30倍以上。此外，在用三（2-羧乙基）膦处理时，客体可以被释放，这减少了将二硫键束缚cur-SH连接到衣壳上。因此，AaLS-IC衣壳可以充当小分子硫醇的容器，并且客体释放可以由还原剂触发。

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