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Journal article

Protein aggregate-ligand binding assays based on microfluidic diffusional separation

Abstract:

The measurement of molecular interactions with pathological protein aggregates, including amyloid fibrils, is of central importance in the context of the development of diagnostic and therapeutic strategies against protein misfolding disorders. Probing such interactions by conventional methods can, however, be challenging because of the supramolecular nature of protein aggregates, their heterogeneity, and their often dynamic nature. Here we demonstrate that direct measurement of diffusion on ...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1002/cbic.201600384

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Physical & Theoretical Chem
Role:
Author
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Funding agency for:
Benesch, J
Grant:
University Research Fellow
Publisher:
Wiley Publisher's website
Journal:
ChemBioChem Journal website
Volume:
17
Issue:
20
Pages:
1920-1924
Publication date:
2016-07-29
Acceptance date:
2016-07-29
DOI:
EISSN:
1439-7633
ISSN:
1439-4227
Pmid:
27472818
Source identifiers:
640790
Language:
English
Keywords:
Pubs id:
pubs:640790
UUID:
uuid:3db31f19-be45-40f6-ae3b-006b3251c881
Local pid:
pubs:640790
Deposit date:
2016-11-11

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