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Supramolecular amplification of amyloid self-assembly by iodination.

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.

journal_name

Nat Commun

journal_title

Nature communications

authors

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

doi

10.1038/ncomms8574

subject

Has Abstract

pub_date

2015-06-30 00:00:00

pages

7574

issn

2041-1723

pii

ncomms8574

journal_volume

6

pub_type

杂志文章

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