The first step of arsenoplatin-1 aggregation in solution unveiled by solving the crystal structure of its protein adduct

Arsenoplatin-1 (AP-1) is an innovative dual-action anticancer agent that contains a platinum(ii) center coordinated to an arsenous acid moiety. We found that AP-1 spontaneously aggregates in aqueous solutions generating oligomeric species of increasing length. Afterward, we succeeded in solving the crystal structure of the adduct formed between the model protein lysozyme and an early AP-1 oligomer that turned out to be a trimer. Remarkably, this crystal structure traps an early stage of AP-1 aggregation offering detailed insight into the molecular process of the oligomer's growth.

Automated summary

Arsenoplatin-1 (AP-1) spontaneously aggregates in aqueous solutions to form oligomeric species, with an early oligomer found to be a trimer in the crystal structure when bound to the model protein lysozyme. This crystal structure captures an early stage of AP-1 aggregation, providing detailed insight into the molecular process of oligomer growth.