Enzyme nanorings

Tsui Fen Chou; Christopher So; Brian R. White; Jonathan C.T. Carlson; Mehmet Sarikaya; Carsten R. Wagner

doi:10.1021/nn800577h

Enzyme nanorings

Tsui Fen Chou, Christopher So, Brian R. White, Jonathan C.T. Carlson, Mehmet Sarikaya, Carsten R. Wagner

Medicinal Chemistry

Research output: Contribution to journal › Article › peer-review

38 Scopus citations

Abstract

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 atomicforce 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.

Original language	English (US)
Pages (from-to)	2519-2525
Number of pages	7
Journal	ACS nano
Volume	2
Issue number	12
DOIs	https://doi.org/10.1021/nn800577h
State	Published - Dec 23 2008

Keywords

Chemical dimerization
Dihydrofolate reductase (DHFR)
Histidine triad nucleotide binding proteins (Hints)
Human hint1
Nanoring
Phosphoramidase
Self-assembly

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10.1021/nn800577h

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abstract = "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 atomicforce 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.",

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T1 - Enzyme nanorings

AU - Chou, Tsui Fen

AU - So, Christopher

AU - White, Brian R.

AU - Carlson, Jonathan C.T.

AU - Sarikaya, Mehmet

AU - Wagner, Carsten R.

PY - 2008/12/23

Y1 - 2008/12/23

N2 - 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 atomicforce 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.

AB - 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 atomicforce 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.

KW - Chemical dimerization

KW - Dihydrofolate reductase (DHFR)

KW - Histidine triad nucleotide binding proteins (Hints)

KW - Human hint1

KW - Nanoring

KW - Phosphoramidase

KW - Self-assembly

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Enzyme nanorings

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