Supramolecular amplification of amyloid self-assembly by iodination

Arianna Bertolani, Lisa Pirrie, Loic Stefan, Nikolay Houbenov, Johannes S. Haataja, Luca Catalano, Giancarlo Terraneo, Gabriele Giancane, Ludovico Valli, Roberto Milani, Olli Ikkala, Giuseppe Resnati, Pierangelo Metrangolo

Research output: Contribution to journalArticleScientificpeer-review

49 Citations (Scopus)
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Amyloid supramolecular assemblies have found widespread exploitation as ordered nanomaterials in a range of applications from materials science to biotechnology. New strategies are, however, required for understanding and promoting mature fibril formation from simple monomer motifs through easy and scalable processes. Noncovalent interactions are key to forming and holding the amyloid structure together. On the other hand, the halogen bond has never been used purposefully to achieve control over amyloid self-assembly. Here we show that single atom replacement of hydrogen with iodine, a halogen-bond donor, in the human calcitonin-derived amyloidogenic fragment DFNKF results in a super-gelator peptide, which forms a strong and shape-persistent hydrogel at 30-fold lower concentration than the wild-type pentapeptide. This is remarkable for such a modest perturbation in structure. Iodination of aromatic amino acids may thus develop as a general strategy for the design of new hydrogels from unprotected peptides and without using organic solvents.
Original languageEnglish
Article number7574
Pages (from-to)1-9
JournalNature Communications
Publication statusPublished - 2015
MoE publication typeA1 Journal article-refereed


  • amyloid

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