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Tuning the self-assembly of the bioactive dipeptide l-carnosine by incorporation of a bulky aromatic substituent
journal contribution
posted on 2023-06-09, 12:54 authored by V Castelletto, G Cheng, Barnaby GreenlandBarnaby Greenland, I W Hamley, P J F HarrisThe dipeptide l-carnosine has a number of important biological properties. Here, we explore the effect of attachment of a bulky hydrophobic aromatic unit, Fmoc [N-(fluorenyl-9-methoxycarbonyl)] on the self-assembly of Fmoc-l-carnosine, i.e., Fmoc-ß-alanine-histidine (Fmoc-ßAH). It is shown that Fmoc-ßAH forms well-defined amyloid fibrils containing ß sheets above a critical aggregation concentration, which is determined from pyrene and ThT fluorescence experiments. Twisted fibrils were imaged by cryogenic transmission electron microscopy. The zinc-binding properties of Fmoc-ßAH were investigated by FTIR and Raman spectroscopy since the formation of metal ion complexes with the histidine residue in carnosine is well-known, and important to its biological roles. Observed changes in the spectra may reflect differences in the packing of the Fmoc-dipeptides due to electrostatic interactions. Cryo-TEM shows that this leads to changes in the fibril morphology. Hydrogelation is also induced by addition of an appropriate concentration of zinc ions. Our work shows that the Fmoc motif can be employed to drive the self-assembly of carnosine into amyloid fibrils.
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Publication status
- Published
File Version
- Published version
Journal
LangmuirISSN
0743-7463Publisher
American Chemical SocietyExternal DOI
Issue
6Volume
27Page range
2980Department affiliated with
- Chemistry Publications
Full text available
- No
Peer reviewed?
- Yes
Legacy Posted Date
2018-04-19First Compliant Deposit (FCD) Date
2018-04-19Usage metrics
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