Issue 36, 2018

Halogen bonding at the wet interfaces of an amyloid peptide structure

Abstract

Amyloid peptide hydrogels are a class of materials of great interest due to their structural simplicity, good performances and easy tuning of their properties by chemical modification. Among the possible modifications, halogenation has not yet been exploited extensively. Here, we report the single-crystal X-ray structure of two dihalogenated derivatives of the amyloidogenic sequence DFNKF. The obtained results show how halogenation is a promising tool to stabilize – through halogen bonds – the wet interface of amyloid structures, to determine an increase in the water uptake, hence the hydrogelation properties of the peptide sequence.

Graphical abstract: Halogen bonding at the wet interfaces of an amyloid peptide structure

Supplementary files

Article information

Article type
Communication
Submitted
20 Jul 2018
Accepted
11 Aug 2018
First published
17 Aug 2018

CrystEngComm, 2018,20, 5321-5326

Halogen bonding at the wet interfaces of an amyloid peptide structure

A. Pizzi, N. Demitri, G. Terraneo and P. Metrangolo, CrystEngComm, 2018, 20, 5321 DOI: 10.1039/C8CE01205A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements