The structural characteristics and the functional evaluation of nanogel

Wakiko Asayama; Masaki Takagi; Shin Ichi Sawada; Nobuyuki Morimoto; Tadashi Narita; Kazunari Akiyoshi

The structural characteristics and the functional evaluation of nanogel

Wakiko Asayama, Masaki Takagi, Shin Ichi Sawada, Nobuyuki Morimoto, Tadashi Narita, Kazunari Akiyoshi

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

Abstract

GroEL or nanogel-mediated folding of β-D-galactosidase was examined. Urea-denatured β-D-galactosidase can spontaneously fold upon the dilution into the low urea concentration (about 15 %). In the presence of GroEL or ALP nanogel, folding of β-D-galactosidase was started by following the dilution. About 50 % of β-D-galactosidase recovered to native structure in both systems of GroEL and dodecyl group-bearing pullulan (ALP) nanogel recovered to native structure. The addition of ATP for GroEL has little effect on refolding. In contrast, the folding was arrested in the presence of CHP nanogels. Even by the addition of methyl-β-cyclodextrin for CHP nanogels, only 15 % of β-D-galactosidase activity recovered. Hydrophobie groups in the nanogels significantly affect chaperon-like activity.

Original language	English
Number of pages	1
Publication status	Published - 2005 Dec 1
Externally published	Yes
Event	54th SPSJ Annual Meeting 2005 - Yokohama, Japan Duration: 2005 May 25 → 2005 May 27

Other

Other	54th SPSJ Annual Meeting 2005
Country	Japan
City	Yokohama
Period	05/5/25 → 05/5/27

Keywords

Artificial molecular chaperon
Cholesterol group-bearing pullulan (CHP)
Protein refolding

ASJC Scopus subject areas

Engineering(all)

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title = "The structural characteristics and the functional evaluation of nanogel",

abstract = "GroEL or nanogel-mediated folding of β-D-galactosidase was examined. Urea-denatured β-D-galactosidase can spontaneously fold upon the dilution into the low urea concentration (about 15 %). In the presence of GroEL or ALP nanogel, folding of β-D-galactosidase was started by following the dilution. About 50 % of β-D-galactosidase recovered to native structure in both systems of GroEL and dodecyl group-bearing pullulan (ALP) nanogel recovered to native structure. The addition of ATP for GroEL has little effect on refolding. In contrast, the folding was arrested in the presence of CHP nanogels. Even by the addition of methyl-β-cyclodextrin for CHP nanogels, only 15 % of β-D-galactosidase activity recovered. Hydrophobie groups in the nanogels significantly affect chaperon-like activity.",

keywords = "Artificial molecular chaperon, Cholesterol group-bearing pullulan (CHP), Protein refolding",

author = "Wakiko Asayama and Masaki Takagi and Sawada, {Shin Ichi} and Nobuyuki Morimoto and Tadashi Narita and Kazunari Akiyoshi",

year = "2005",

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note = "54th SPSJ Annual Meeting 2005 ; Conference date: 25-05-2005 Through 27-05-2005",

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T1 - The structural characteristics and the functional evaluation of nanogel

AU - Asayama, Wakiko

AU - Takagi, Masaki

AU - Sawada, Shin Ichi

AU - Morimoto, Nobuyuki

AU - Narita, Tadashi

AU - Akiyoshi, Kazunari

PY - 2005/12/1

Y1 - 2005/12/1

N2 - GroEL or nanogel-mediated folding of β-D-galactosidase was examined. Urea-denatured β-D-galactosidase can spontaneously fold upon the dilution into the low urea concentration (about 15 %). In the presence of GroEL or ALP nanogel, folding of β-D-galactosidase was started by following the dilution. About 50 % of β-D-galactosidase recovered to native structure in both systems of GroEL and dodecyl group-bearing pullulan (ALP) nanogel recovered to native structure. The addition of ATP for GroEL has little effect on refolding. In contrast, the folding was arrested in the presence of CHP nanogels. Even by the addition of methyl-β-cyclodextrin for CHP nanogels, only 15 % of β-D-galactosidase activity recovered. Hydrophobie groups in the nanogels significantly affect chaperon-like activity.

AB - GroEL or nanogel-mediated folding of β-D-galactosidase was examined. Urea-denatured β-D-galactosidase can spontaneously fold upon the dilution into the low urea concentration (about 15 %). In the presence of GroEL or ALP nanogel, folding of β-D-galactosidase was started by following the dilution. About 50 % of β-D-galactosidase recovered to native structure in both systems of GroEL and dodecyl group-bearing pullulan (ALP) nanogel recovered to native structure. The addition of ATP for GroEL has little effect on refolding. In contrast, the folding was arrested in the presence of CHP nanogels. Even by the addition of methyl-β-cyclodextrin for CHP nanogels, only 15 % of β-D-galactosidase activity recovered. Hydrophobie groups in the nanogels significantly affect chaperon-like activity.

KW - Artificial molecular chaperon

KW - Cholesterol group-bearing pullulan (CHP)

KW - Protein refolding

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