Enzyme Nanorings

被引：36

作者：

Chou, Tsui-Fen ^{[1
]}

So, Christopher ^{[3
]}

White, Brian R. ^{[1
]}

Carlson, Jonathan C. T. ^{[1
]}

Sarikaya, Mehmet ^{[3
]}

Wagner, Carston R. ^{[1
,2
]}

机构：

[1] Univ Minnesota, Dept Med Chem, Minneapolis, MN 55455 USA

[2] Univ Minnesota, Dept Chem, Minneapolis, MN 55455 USA

[3] Univ Washington, Dept Mat Sci & Engn & Chem Engn, Genetically Engn Mat Sci & Engn Ctr, Seattle, WA 98195 USA

来源：

ACS NANO | 2008年 / 2卷 / 12期

关键词：

nanoring; histidine triad nucleotide binding proteins (Hints); phosphoramidase; human Hint1; dihydrofolate reductase (DHFR); self-assembly; chemical dimerization;

D O I：

10.1021/nn800577h

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

We have demonstrated that nanostructures, and in particular nanorings incorporating a homodimeric enzyme, can be prepared by chemically induced self-assembly of dihydrofolate reductase (DHFR)-histidine triad nucleotide binding 1 (Hint1) fusion proteins. The dimensions of the nanorings were found by static light scattering and atomic force microscopy studies to be dependent on the length and composition of the peptide linking the fusion proteins, ranging in size from 10 to 70 nm in diameter and 64 to 740 kDa. The catalytic efficiency of the nanorings was found to be dependent on ring size, thus suggesting that the arrangement of supermolecular assemblies of enzymes may be used to control their catalytic parameters.

引用

页码：2519 / 2525

页数：7

共 16 条

[1] Designing protein dimerizers: The importance of ligand conformational equilibria [J].

Carlson, JCT ;

Kanter, A ;

Thuduppathy, GR ;

Cody, V ;

Pineda, PE ;

McIvor, RS ;

Wagner, CR .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2003, 125 (06) :1501-1507

[2] Chemically controlled self-assembly of protein nanorings [J].

Carlson, Jonathan C. T. ;

Jena, Sidhartha S. ;

Flenniken, Michelle ;

Chou, Tsui-fen ;

Siegel, Ronald A. ;

Wagner, Carston R. .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2006, 128 (23) :7630-7638

[3] 31P NMR and genetic analysis establish hinT as the only Escherchia coli purine nucleoside phosphoramidase and as essential for growth under high salt conditions [J].

Chou, TF ;

Bieganowski, P ;

Shilinski, K ;

Cheng, JL ;

Brenner, C ;

Wagner, CR .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (15) :15356-15361

[4] Engineered monomeric human histidine triad nucleotide-binding protein 1 hydrolyzes fluorogenic acyl-adenylate and lysyl-tRNA synthetase-generated lysyl-adenylate [J].

Chou, Tsui-Fen ;

Tikh, Ilya B. ;

Horta, Bruno A. C. ;

Ghosh, Brahma ;

De Alencastro, Ricardo B. ;

Wagner, Carston R. .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2007, 282 (20) :15137-15147

[5] Phosphoramidate pronucleotides:: A comparison of the phosphoramidase substrate specificity of human and Escherichia coli histidine triad nucleotide binding proteins [J].

Chou, Tsui-Fen ;

Baraniak, Janina ;

Kaczmarek, Renata ;

Zhou, Xin ;

Cheng, Jilin ;

Ghosh, Brahma ;

Wagner, Carston R. .

MOLECULAR PHARMACEUTICS, 2007, 4 (02) :208-217

[6] Lysyl-tRNA synthetase-generated lysyl-adenylate is a substrate for histidine triad nucleotide binding proteins [J].

Chou, Tsui-Fen ;

Wagner, Carston R. .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2007, 282 (07) :4719-4727

[7] A model for self-assembly in solution [J].

Ercolani, G .

JOURNAL OF PHYSICAL CHEMISTRY B, 2003, 107 (21) :5052-5057

[8] Improved calculation of rotational diffusion and intrinsic viscosity of bead models for macromolecules and nanoparticles [J].

Garcia de la Torre, J. ;

del Rio Echenique, G. ;

Ortega, A. .

JOURNAL OF PHYSICAL CHEMISTRY B, 2007, 111 (05) :955-961

[9] Designed protein-protein association [J].

Grueninger, Dirk ;

Treiber, Nora ;

Ziegler, Mathias O. P. ;

Koetter, Jochen W. A. ;

Schulze, Monika-Sarah ;

Schulz, Georg E. .

SCIENCE, 2008, 319 (5860) :206-209

[10] ULTRALARGE ATOMICALLY FLAT TEMPLATE-STRIPPED AU SURFACES FOR SCANNING PROBE MICROSCOPY [J].

HEGNER, M ;

WAGNER, P ;

SEMENZA, G .

SURFACE SCIENCE, 1993, 291 (1-2) :39-46

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