Supramolecular amplification of amyloid self-assembly by iodination - Université de Lorraine Accéder directement au contenu
Article Dans Une Revue Nature Communications Année : 2015

Supramolecular amplification of amyloid self-assembly by iodination

Résumé

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.
Fichier principal
Vignette du fichier
Stefan_NatureComm_2015.pdf (2.03 Mo) Télécharger le fichier
Origine : Fichiers éditeurs autorisés sur une archive ouverte
Loading...

Dates et versions

hal-02086232 , version 1 (01-04-2019)

Identifiants

Citer

Arianna Bertolani, Lisa Pirrie, Loïc Stefan, Nikolay Houbenov, Johannes S Haataja, et al.. Supramolecular amplification of amyloid self-assembly by iodination. Nature Communications, 2015, 6 (1), ⟨10.1038/ncomms8574⟩. ⟨hal-02086232⟩
34 Consultations
98 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More