Nanoparticle self-assembly directed by antagonistic kinase and phosphatase activities

被引：41

作者：

von Maltzahn, Geoffrey

Min, Dal-Hee

Zhang, Yingxin

Park, Ji-Ho

Harris, Todd J.

Sailor, Michael

Bhatia, Sangeeta N.

机构：

[1] Harvard Univ, MIT, Div Hlth Sci & Technol, Cambridge, MA 02139 USA

[2] Brigham & Womens Hosp, MIT, Boston, MA 02115 USA

[3] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA

来源：

ADVANCED MATERIALS | 2007年 / 19卷 / 21期

关键词：

D O I：

10.1002/adma.200701183

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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.

引用

收藏

页码：3579 / +

页数：6

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