Structural evolution of human recombinant αB-crystallin under UV irradiation

Masaaki Sugiyama, Noriko Fujii, Yukio Morimoto, Sakie Kurabayashi, Martin E. Vigild, Tatsuo Nakagawa, Takashi Sato, Keiji Itoh, Kazuhiro Mori, Toshiharu Fukunaga

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

External stresses cause certain proteins to lose their regular structure and aggregate. In order to clarify this abnormal aggregation process, a structural evolution of human recombinant αB-crystalhn under UV irradiation was observed with in situ small-angle neutron scattering. The abnormal aggregation process was identified to fall in three time zones: incubation, aggregation, and saturation. During the incubation time, the size of aggregates was almost unchanged but a deformation in the local structure was developing. After the incubation time, abnormal aggregation proceed. When the volume of the aggregates reached around twice the size as that of the initial aggregates, the aggregation rate slowed down, which marked the onset of saturation.

Original languageEnglish
Pages (from-to)431-434
Number of pages4
JournalBiomacromolecules
Volume9
Issue number2
DOIs
Publication statusPublished - Feb 1 2008
Externally publishedYes

ASJC Scopus subject areas

  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry

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  • Cite this

    Sugiyama, M., Fujii, N., Morimoto, Y., Kurabayashi, S., Vigild, M. E., Nakagawa, T., Sato, T., Itoh, K., Mori, K., & Fukunaga, T. (2008). Structural evolution of human recombinant αB-crystallin under UV irradiation. Biomacromolecules, 9(2), 431-434. https://doi.org/10.1021/bm7004802