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

薬科学科

研究成果: Paper › 査読

抄録

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.

本文言語	English
ページ	4719-4720
ページ数	2
出版ステータス	Published - 2005 12月 1
イベント	54th SPSJ Symposium on Macromolecules - Yamagata, Japan 継続期間: 2005 9月 20 → 2005 9月 22

Other

Other	54th SPSJ Symposium on Macromolecules
国/地域	Japan
City	Yamagata
Period	05/9/20 → 05/9/22

ASJC Scopus subject areas

工学（全般）

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引用スタイル

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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",

month = dec,

day = "1",

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 - 2005/12/1

Y1 - 2005/12/1

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

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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

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