Imperial College London

Dr Kuimova

Faculty of Natural SciencesDepartment of Chemistry

Reader in Chemical Physics
 
 
 
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Contact

 

+44 (0)20 7594 8558m.kuimova

 
 
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Location

 

207BMolecular Sciences Research HubWhite City Campus

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Summary

 

Publications

Citation

BibTex format

@article{Kuimova:2017:10.1016/j.biomaterials.2017.06.009,
author = {Kuimova, MK and Kubankova, M and Lopez, Duarte and Bull and Vadukul and Serpell and de, Saint Victor and Stride},
doi = {10.1016/j.biomaterials.2017.06.009},
journal = {Biomaterials},
pages = {195--201},
title = {Probing supramolecular protein assembly using covalently attached fluorescent molecular rotors},
url = {http://dx.doi.org/10.1016/j.biomaterials.2017.06.009},
volume = {139},
year = {2017}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Changes in microscopic viscosity and macromolecular crowding accompany the transition of proteins from their monomeric forms into highly organised fibrillar states. Previously, we have demonstrated that viscosity sensitive fluorophores termed ‘molecular rotors’, when freely mixed with monomers of interest, are able to report on changes in microrheology accompanying amyloid formation, and measured an increase in rigidity of approximately three orders of magnitude during aggregation of lysozyme and insulin. Here we extend this strategy by covalently attaching molecular rotors to several proteins capable of assembly into fibrils, namely lysozyme, fibrinogen and amyloid-β peptide (Aβ(1–42)). We demonstrate that upon covalent attachment the molecular rotors can successfully probe supramolecular assembly in vitro. Importantly, our new strategy has wider applications in cellulo and in vivo, since covalently attached molecular rotors can be successfully delivered in situ and will colocalise with the aggregating protein, for example inside live cells. This important advantage allowed us to follow the microscopic viscosity changes accompanying blood clotting and during Aβ(1–42) aggregation in live SH-SY5Y cells. Our results demonstrate that covalently attached molecular rotors are a widely applicable tool to study supramolecular protein assembly and can reveal microrheological features of aggregating protein systems both in vitro and in cellulo not observable through classical fluorescent probes operating in light switch mode.
AU - Kuimova,MK
AU - Kubankova,M
AU - Lopez,Duarte
AU - Bull
AU - Vadukul
AU - Serpell
AU - de,Saint Victor
AU - Stride
DO - 10.1016/j.biomaterials.2017.06.009
EP - 201
PY - 2017///
SN - 1878-5905
SP - 195
TI - Probing supramolecular protein assembly using covalently attached fluorescent molecular rotors
T2 - Biomaterials
UR - http://dx.doi.org/10.1016/j.biomaterials.2017.06.009
UR - http://hdl.handle.net/10044/1/49115
VL - 139
ER -