Aggregation dynamics of laminin-1 in a physiological solution: A time-resolved static light scattering study

被引:9
|
作者
Onuma, K [1 ]
Kanzaki, N [1 ]
机构
[1] Natl Inst Adv Ind Sci & Technol, Inst Human Sci & Biomed Engn, Tsukuba, Ibaraki 3058562, Japan
关键词
fractal dimension; static light scattering; proteins;
D O I
10.1016/j.jcrysgro.2005.07.035
中图分类号
O7 [晶体学];
学科分类号
0702 ; 070205 ; 0703 ; 080501 ;
摘要
The aggregation of laminin-1 in a physiological solution was observed using time-resolved static light scattering. In a Solution containing 150 mM of NaCl and 1 mM of CaCl2, with a pH of 7.2 buffered by 50 mM Tris, and maintained at 25 degrees C, the weight-averaged mass (molecular weight) M,, and radius of gyration R., of the aggregate were measured at 10s intervals. The aggregation kinetics changed from reaction-limited Cluster aggregation (RLCA) to diffusion-limited cluster aggregation (DLCA) over time. The fractal dimension estimated in the DLCA regime was 1.71 from the M(w)similar to R-g(df) relationship, which is consistent with the d(f) of 1.75 obtained from an R(g)similar to t(1/df), plot. Direct calculation of d(f) using the scattering intensity and scattering vector revealed that df gradually increased over time in the DLCA regime, suggesting that spontaneous restructuring of the aggregate had Occurred. This restructuring would have been caused by hydrophobic contact in the aggregate. The form factor of the aggregate was well fitted by a linear random coil model and not by a simple spherical model. (c) 2005 Elsevier B.V. All rights reserved.
引用
收藏
页码:530 / 537
页数:8
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