通过原子力显微镜监测免疫球蛋白轻链淀粉样纤维的组装
Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy.
作者信息
Ionescu-Zanetti C, Khurana R, Gillespie J R, Petrick J S, Trabachino L C, Minert L J, Carter S A, Fink A L
机构信息
Department of Physics, University of California, Santa Cruz, CA 95064, USA.
出版信息
Proc Natl Acad Sci U S A. 1999 Nov 9;96(23):13175-9. doi: 10.1073/pnas.96.23.13175.
Abstract
Aggregation of Ig light chains to form amyloid fibrils is a characteristic feature of light-chain amyloidosis, a light-chain deposition disease. A recombinant variable domain of the light chain SMA was used to form amyloid fibrils in vitro. Fibril formation was monitored by atomic force microscopy imaging. Single filaments 2.4 nm in diameter were predominant at early times; protofibrils 4.0 nm in diameter were predominant at intermediate times; type I and type II fibrils 8.0 nm and 6.0 nm in diameter, respectively, were predominant at the endpoints. The increase in number of fibrils correlated with increased binding of the fluorescent dye thioflavin T. The fibrils and protofibrils showed a braided structure, suggesting that their formation involves the winding of protofibrils and filaments, respectively. These observations support a model in which two filaments combine to form a protofibril, two protofibrils intertwine to form a type I fibril, and three filaments form a type II fibril.
摘要
免疫球蛋白轻链聚集成淀粉样纤维是轻链淀粉样变性（一种轻链沉积病）的特征性表现。轻链SMA的重组可变结构域用于在体外形成淀粉样纤维。通过原子力显微镜成像监测纤维形成过程。早期直径为2.4nm的单丝占主导；中期直径为4.0nm的原纤维占主导；终点时直径分别为8.0nm的I型纤维和6.0nm的II型纤维占主导。纤维数量的增加与荧光染料硫黄素T的结合增加相关。纤维和原纤维呈现出辫状结构，表明它们的形成分别涉及原纤维和单丝的缠绕。这些观察结果支持一种模型，即两条单丝结合形成一条原纤维，两条原纤维相互缠绕形成I型纤维，三条单丝形成II型纤维。
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