Assembly of histidine-rich protein materials controlled through divalent cations

Hèctor López-Laguna, Ugutz Unzueta, Oscar Conchillo-Solé, Alejandro Sánchez-Chardi, Mireia Pesarrodona, Olivia Cano-Garrido, Eric Voltà, Laura Sánchez-García, Naroa Serna, Paolo Saccardo, Ramón Mangues, Antonio Villaverde, Esther Vázquez

Research output: Contribution to journalArticleResearch

25 Citations (Scopus)


© 2018 Acta Materialia Inc. Nanostructured protein materials show exciting biomedical applications, since both structure and function can be genetically programmed. In particular, self-assembling histidine-rich proteins benefit from functional plasticity that allows the generation of protein-only nanoparticles for cell targeted drug delivery. However, the rational development of constructs with improved functions is limited by a poor control of the oligomerization process. By exploring cross-interactions between histidine-tagged building blocks, we have identified a critical architectonic role of divalent cations. The obtained data instruct about how histidine-rich protein materials can be assembled, disassembled and reassembled within the nanoscale through the stoichiometric manipulation of divalent ions, in a biochemical approach to biomaterials design. Statement of Significance: Divalent metal and non-metal cations such as Ni2+, Cu2+ Ca2+ and Zn2+ have been identified as unexpected molecular tools to control the assembling, disassembling and reassembling of histidine-rich protein materials at the nanoscale. Their stoichiometric manipulation allows generating defined protein-protein cross-molecular contacts between building blocks, for a powerful nano-biochemical manipulation of the material's architecture.
Original languageEnglish
Pages (from-to)257-264
JournalActa Biomaterialia
Publication statusPublished - 1 Jan 2019


  • Controlled oligomerization
  • Functional materials
  • Genetic design
  • Nanoparticles
  • Protein materials


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