Sugiyama Masaaki, Fujii Noriko, Morimoto Yukio, Kurabayashi Sakie, Vigild Martin E, Nakagawa Tatsuo, Sato Takashi, Itoh Keiji, Mori Kazuhiro, Fukunaga Toshiharu
Research Reactor Institute, Kyoto University, Osaka 590-0494, Japan.
Biomacromolecules. 2008 Feb;9(2):431-4. doi: 10.1021/bm7004802. Epub 2008 Jan 23.
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 alphaB-crystallin 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.
外部压力会导致某些蛋白质失去其规则结构并发生聚集。为了阐明这种异常聚集过程，利用原位小角中子散射观察了人重组αB-晶状体蛋白在紫外线照射下的结构演变。异常聚集过程被确定分为三个时间段：潜伏期、聚集期和饱和期。在潜伏期，聚集体的大小几乎不变，但局部结构正在发生变形。潜伏期过后，异常聚集开始。当聚集体的体积达到初始聚集体大小的两倍左右时，聚集速率减慢，这标志着饱和期的开始。
