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Issue 36, 2018
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Halogen bonding at the wet interfaces of an amyloid peptide structure

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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

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Publication details

The article was received on 20 Jul 2018, accepted on 11 Aug 2018 and first published on 17 Aug 2018


Article type: Communication
DOI: 10.1039/C8CE01205A
Citation: CrystEngComm, 2018,20, 5321-5326

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    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

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