Nanoparticle self-assembly directed by antagonistic kinase and phosphatase activities
Superparamagnetic Fe3O4 nanoparticles (NPs) are engineered to reversibly self-assemble in response to antagonistic enzyme inputs. Tyrosine kinase activity directs substrate-NPs and SH2 domain-NPs to coalesce via polyvalent SH2- phosphopeptide binding. Phosphatase antagonizes this process and directs NP dispersion. By coupling assembly to substrate phosphorylation, the kinase activity is imaged via quantitative T2 relaxation changes in MRI.
- Publisher
- WILEY-V C H VERLAG GMBH
- Issue Date
- 2007-11
- Language
- English
- Article Type
- Article
- Keywords
TYROSINE KINASE; MOLECULAR-INTERACTIONS; SIGNAL-TRANSDUCTION; GOLD NANOPARTICLES; QUANTUM DOTS; PHOSPHORYLATION; MULTIVALENT; NANOSENSORS; RECEPTORS; DELIVERY
- Citation
ADVANCED MATERIALS, v.19, no.21, pp.3579 - 3579
- ISSN
- 0935-9648
- Appears in Collection
- CH-Journal Papers(저널논문)BiS-Journal Papers(저널논문)
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