Tarasevich Barbara J, Lea Scott, Bernt William, Engelhard Mark H, Shaw Wendy J
Pacific Northwest National Laboratory, Richland, WA 99352, USA.
Biopolymers. 2009 Feb;91(2):103-7. doi: 10.1002/bip.21095.
Amelogenin is a unique protein that self-assembles into spherical aggregates called "nanospheres" and is believed to be involved in controlling the formation of the highly anisotropic and ordered hydroxyapatite crystallites that form enamel. The adsorption behavior of amelogenin onto substrates is of great interest because protein-surface interactions are critical to its function. We report studies of the adsorption of amelogenin onto self-assembled monolayers containing COOH end group functionality as well as single crystal fluoroapatite, a biologically relevant surface. We found that although our solutions contained only nanospheres of narrow size distribution, smaller structures such as dimers or trimers were observed on the hydrophilic surfaces. This suggests that amelogenin can adsorb onto surfaces as small structures that "shed" or disassemble from the nanospheres that are present in solution.
釉原蛋白是一种独特的蛋白质，它能自组装成称为“纳米球”的球形聚集体，并且被认为参与控制形成牙釉质的高度各向异性且有序的羟基磷灰石微晶。釉原蛋白在底物上的吸附行为备受关注，因为蛋白质与表面的相互作用对其功能至关重要。我们报告了关于釉原蛋白在含有COOH端基官能团的自组装单分子层以及单晶氟磷灰石（一种具有生物学相关性的表面）上的吸附研究。我们发现，尽管我们的溶液中仅含有尺寸分布狭窄的纳米球，但在亲水性表面上观察到了诸如二聚体或三聚体等较小的结构。这表明釉原蛋白可以以从小球上“脱落”或从溶液中存在的纳米球上解离下来的小结构形式吸附到表面上。
