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 and Pierangelo Metrangolo ()
Additional contact information
Arianna Bertolani: Laboratory of Nanostructured Fluorinated Materials (NFMLab), Materials, and Chemical Engineering ‘Giulio Natta’, Politecnico di Milano
Lisa Pirrie: Laboratory of Nanostructured Fluorinated Materials (NFMLab), Materials, and Chemical Engineering ‘Giulio Natta’, Politecnico di Milano
Loic Stefan: Laboratory of Nanostructured Fluorinated Materials (NFMLab), Materials, and Chemical Engineering ‘Giulio Natta’, Politecnico di Milano
Nikolay Houbenov: Aalto University
Johannes S. Haataja: Aalto University
Luca Catalano: Laboratory of Nanostructured Fluorinated Materials (NFMLab), Materials, and Chemical Engineering ‘Giulio Natta’, Politecnico di Milano
Giancarlo Terraneo: Laboratory of Nanostructured Fluorinated Materials (NFMLab), Materials, and Chemical Engineering ‘Giulio Natta’, Politecnico di Milano
Gabriele Giancane: Università del Salento
Ludovico Valli: Università del Salento
Roberto Milani: VTT-Technical Research Centre of Finland
Olli Ikkala: Aalto University
Giuseppe Resnati: Laboratory of Nanostructured Fluorinated Materials (NFMLab), Materials, and Chemical Engineering ‘Giulio Natta’, Politecnico di Milano
Pierangelo Metrangolo: Laboratory of Nanostructured Fluorinated Materials (NFMLab), Materials, and Chemical Engineering ‘Giulio Natta’, Politecnico di Milano

Nature Communications, 2015, vol. 6, issue 1, 1-9

Abstract: Abstract 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.

Date: 2015
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms8574 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8574

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms8574

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().