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.

Autore Pugliese

• Giancane Gabriele , Valli Ludovico

Tutti gli autori

• Bertolani A. , Pirrie L.A. , Stefan L. , Houbenov N. , Haataja J.S. , Catalano L. , Terraneo G. , Giancane G. , Valli L. , Milani R. , Ikkala O. , Resnati G. , Metrangolo P.

Titolo volume/Rivista

NATURE COMMUNICATIONS

Anno di pubblicazione

2015

ISSN

2041-1723

ISBN

Non Disponibile

Numero di citazioni Wos

26

Ultimo Aggiornamento Citazioni

22/04/2018

Numero di citazioni Scopus

22

Ultimo Aggiornamento Citazioni

22/04/2018

Settori ERC

Non Disponibile

Codici ASJC

Non Disponibile