Reversible loading of thiol-modified curcumin in an engineered protein capsid
| Autor: | K. J. Woycechowsky, Qing-Xiang Guo, G. C. Thomas |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
Tris
Aquifex aeolicus biology Chemistry Reducing agent General Chemical Engineering macromolecular substances 02 engineering and technology General Chemistry 010402 general chemistry 021001 nanoscience & nanotechnology biology.organism_classification 01 natural sciences Combinatorial chemistry Lumazine synthase 0104 chemical sciences Adduct Crystallography chemistry.chemical_compound Capsid Covalent bond biology.protein 0210 nano-technology Cysteine |
| Zdroj: | RSC Advances. 7:34676-34686 |
| ISSN: | 2046-2069 |
| DOI: | 10.1039/c7ra05890j |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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