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 conferencePaperpeer-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 languageEnglish
Number of pages1
Publication statusPublished - 2005 Dec 1
Externally publishedYes
Event54th SPSJ Annual Meeting 2005 - Yokohama, Japan
Duration: 2005 May 252005 May 27

Other

Other54th SPSJ Annual Meeting 2005
CountryJapan
CityYokohama
Period05/5/2505/5/27

Keywords

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

ASJC Scopus subject areas

  • Engineering(all)

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