Moradian-Oldak J, Simmer J P, Lau E C, Diekwisch T, Slavkin H C, Fincham A G
Center for Craniofacial Molecular Biology, School of Dentistry, University of Southern California, Los Angeles 90033, USA.
Connect Tissue Res. 1995;32(1-4):125-30. doi: 10.3109/03008209509013714.
The present paper reviews some recent data on the aggregation properties of a recombinant amelogenin using dynamic light scattering, transmission electron microscopy, atomic force microscopy, and size exclusion chromatography. It was found that the recombinant amelogenin M179 molecules in solution form spherical monodisperse aggregates (15-20 nm) which are predominantly stabilized by intermolecular hydrophobic interactions while their surfaces are charged, carrying the hydrophilic carboxy-terminal sequence. We concluded that the spherical aggregates represent the "stippled materials" secreted by the ameloblasts at the mineralization front. We further speculate that the self-assembly process in the formation of amelogenin aggregates may play a primary role in the structural organization of mineralizing enamel.
本文利用动态光散射、透射电子显微镜、原子力显微镜和尺寸排阻色谱法,综述了一些关于重组牙釉蛋白聚集特性的最新数据。研究发现,溶液中的重组牙釉蛋白M179分子形成球形单分散聚集体(15 - 20纳米),这些聚集体主要通过分子间疏水相互作用稳定,而其表面带电荷,携带亲水性的羧基末端序列。我们得出结论,球形聚集体代表成釉细胞在矿化前沿分泌的“点状物质”。我们进一步推测,牙釉蛋白聚集体形成过程中的自组装过程可能在矿化牙釉质的结构组织中起主要作用。