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Probing supramolecular protein assembly using covalently attached fluorescent molecular rotors

Abstract:

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...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Funding agency for:
de Saint Victor, M
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Funding agency for:
Stride, E
Publisher:
Elsevier Publisher's website
Journal:
Biomaterials Journal website
Volume:
139
Pages:
195-201
Publication date:
2017-06-07
Acceptance date:
2017-06-05
DOI:
EISSN:
1878-5905
ISSN:
0142-9612
Pubs id:
pubs:702202
URN:
uri:e66eed6f-f511-4a47-b106-94f6879c0525
UUID:
uuid:e66eed6f-f511-4a47-b106-94f6879c0525
Local pid:
pubs:702202

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