Affinity control of immobilized metal ligands with proteins using thermoresponsive nanogel-like interfaces

Akihiko Kikuchi; Tetsuya Endo; Jun Kobayashi; Hideko Kanazawa; Kiyotaka Sakai; Teruo Okano

Affinity control of immobilized metal ligands with proteins using thermoresponsive nanogel-like interfaces

Akihiko Kikuchi, Tetsuya Endo, Jun Kobayashi, Hideko Kanazawa, Kiyotaka Sakai, Teruo Okano

Department of Materials Science and Technology

Research output: Contribution to conference › Paper › peer-review

Abstract

In the present research, we newly developed thermoresponsive nanobio interfaces for possible applications in affinity regulations. We introduced thermoresponsive polymers having metal chelating segments (iminodiacetic acid moiety on the side chains) onto animated silica beads surfaces. Utilizing thermoresponsive expanding-contracting changes of poly(N-isopropylacrylamide) on the bead surfaces, we succeeded in on-off regulation of specific affinity interactions between immobilized metal ligands and lysozyme having one histidine residue. The obtained results suggest that affinity modulation can be achieved by utilizing thermally regulated polymer chain hydration changes without any use of competitive agents.

Original language	English
Pages	4719-4720
Number of pages	2
Publication status	Published - 2005
Event	54th SPSJ Symposium on Macromolecules - Yamagata, Japan Duration: 20 Sept 2005 → 22 Sept 2005

Conference

Conference	54th SPSJ Symposium on Macromolecules
Country/Territory	Japan
City	Yamagata
Period	20/09/05 → 22/09/05

Keywords

Chromatography
Immobilized metal affinity ligands
Poly(N-isopropylacrylamide)
Protein separation
Ultrathin polymer interfaces

Cite this

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title = "Affinity control of immobilized metal ligands with proteins using thermoresponsive nanogel-like interfaces",

abstract = "In the present research, we newly developed thermoresponsive nanobio interfaces for possible applications in affinity regulations. We introduced thermoresponsive polymers having metal chelating segments (iminodiacetic acid moiety on the side chains) onto animated silica beads surfaces. Utilizing thermoresponsive expanding-contracting changes of poly(N-isopropylacrylamide) on the bead surfaces, we succeeded in on-off regulation of specific affinity interactions between immobilized metal ligands and lysozyme having one histidine residue. The obtained results suggest that affinity modulation can be achieved by utilizing thermally regulated polymer chain hydration changes without any use of competitive agents.",

keywords = "Chromatography, Immobilized metal affinity ligands, Poly(N-isopropylacrylamide), Protein separation, Ultrathin polymer interfaces",

author = "Akihiko Kikuchi and Tetsuya Endo and Jun Kobayashi and Hideko Kanazawa and Kiyotaka Sakai and Teruo Okano",

year = "2005",

language = "English",

pages = "4719--4720",

note = "54th SPSJ Symposium on Macromolecules ; Conference date: 20-09-2005 Through 22-09-2005",

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TY - CONF

T1 - Affinity control of immobilized metal ligands with proteins using thermoresponsive nanogel-like interfaces

AU - Kikuchi, Akihiko

AU - Endo, Tetsuya

AU - Kobayashi, Jun

AU - Kanazawa, Hideko

AU - Sakai, Kiyotaka

AU - Okano, Teruo

PY - 2005

Y1 - 2005

N2 - In the present research, we newly developed thermoresponsive nanobio interfaces for possible applications in affinity regulations. We introduced thermoresponsive polymers having metal chelating segments (iminodiacetic acid moiety on the side chains) onto animated silica beads surfaces. Utilizing thermoresponsive expanding-contracting changes of poly(N-isopropylacrylamide) on the bead surfaces, we succeeded in on-off regulation of specific affinity interactions between immobilized metal ligands and lysozyme having one histidine residue. The obtained results suggest that affinity modulation can be achieved by utilizing thermally regulated polymer chain hydration changes without any use of competitive agents.

AB - In the present research, we newly developed thermoresponsive nanobio interfaces for possible applications in affinity regulations. We introduced thermoresponsive polymers having metal chelating segments (iminodiacetic acid moiety on the side chains) onto animated silica beads surfaces. Utilizing thermoresponsive expanding-contracting changes of poly(N-isopropylacrylamide) on the bead surfaces, we succeeded in on-off regulation of specific affinity interactions between immobilized metal ligands and lysozyme having one histidine residue. The obtained results suggest that affinity modulation can be achieved by utilizing thermally regulated polymer chain hydration changes without any use of competitive agents.

KW - Chromatography

KW - Immobilized metal affinity ligands

KW - Poly(N-isopropylacrylamide)

KW - Protein separation

KW - Ultrathin polymer interfaces

UR - http://www.scopus.com/inward/record.url?scp=33645580175&partnerID=8YFLogxK

M3 - Paper

AN - SCOPUS:33645580175

SP - 4719

EP - 4720

T2 - 54th SPSJ Symposium on Macromolecules

Y2 - 20 September 2005 through 22 September 2005

ER -

Affinity control of immobilized metal ligands with proteins using thermoresponsive nanogel-like interfaces

Abstract

Conference

Keywords

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