Imperial College London
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Dr Francesco A. Aprile

Faculty of Natural Sciences, Department of Chemistry

Lecturer in Chemistry
 
 
 
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Contact

 

+44 (0)20 7594 5545f.aprile Website

 
 
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Location

 

110FMolecular Sciences Research HubWhite City Campus

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Summary

 

Publications

Citation

BibTex format

@article{Ge:2022:10.1021/acschemneuro.2c00077,
author = {Ge, Y and Masoura, A and Yang, J and Aprile, F},
doi = {10.1021/acschemneuro.2c00077},
journal = {ACS Chemical Neuroscience},
pages = {1714--1718},
title = {A chemical mutagenesis approach to insert post-translational modifications in aggregation-prone proteins},
url = {http://dx.doi.org/10.1021/acschemneuro.2c00077},
volume = {13},
year = {2022}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Neurodegenerative diseases are a class of disorders linked to the formation in the nervous system of fibrillar protein aggregates called amyloids. This aggregation process is affected by a variety of post-translational modifications, whose specific mechanisms are not fully understood yet. Emerging chemical mutagenesis technology is currently striving to address the challenge of introducing protein post-translational modifications, while maintaining the stability and solubility of the proteins during the modification reaction. Several amyloidogenic proteins are highly aggregation-prone, and current modification procedures can lead to unexpected precipitation of these proteins, affecting their yield and downstream characterization. Here, we present a method for maintaining amyloidogenic protein solubility during chemical mutagenesis. As proof-of-principle, we applied our method to mimic the phosphorylation of serine-26 and the acetylation of lysine-28 of the 40-residue long variant of amyloid-β peptide, whose aggregation is linked to Alzheimer’s disease.
AU  - Ge,Y
AU  - Masoura,A
AU  - Yang,J
AU  - Aprile,F
DO  - 10.1021/acschemneuro.2c00077
EP  - 1718
PY  - 2022///
SN  - 1948-7193
SP  - 1714
TI  - A chemical mutagenesis approach to insert post-translational modifications in aggregation-prone proteins
T2  - ACS Chemical Neuroscience
UR  - http://dx.doi.org/10.1021/acschemneuro.2c00077
UR  - https://pubs.acs.org/doi/10.1021/acschemneuro.2c00077
UR  - http://hdl.handle.net/10044/1/97387
VL  - 13
ER  -
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