A gravimetric analysis of protein-oligosaccharide interactions.
A gravimetric analysis of protein-oligosaccharide interactions.
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蛋白质-寡糖相互作用的重量分析。
DOI：
10.1042/bst0310349
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发表时间：
2003
影响因子：
3.9
通讯作者：
D. Fernig
中科院分区：
文献类型：
--
作者：
T. Rudd;J. Gallagher;D. Ron;R. Nichols;D. Fernig
使用石英晶体微天平-耗散（QCM-D）观察了固定化肝素衍生八糖和生长因子之间的相互作用。该装置可以测量结合到八糖表面的生长因子的量以及表面耗散的变化。耗散是粘附材料如何“阻尼”表面振动的量度。八糖通过它们的还原末端被中间体烷基硫醇分子锚定，烷基硫醇分子通过硫醇基团共价结合到晶体表面。正如预期的那样，硫酸肝素结合生长因子与八糖结合，但是对于不同的生长因子，每单位耗散变化结合的生长因子质量的变化是不同的。因此，表明各种生长因子-八糖复合物的结构是不同的，表明耗散的变化可以深入了解寡糖-生长因子复合物的结构、取向和包装。
Interactions between an immobilized, heparin-derived octasaccharide and growth factors have been observed using a quartz crystal microbalance-dissipation (QCM-D). This device can measure the amount of growth factors binding to the octasaccharide surface and also the change of dissipation of the surface. Dissipation is a measure of how the adhered material 'damps' the surface vibrations. The octasaccharides were anchored through their reducing ends by the intermediary of the alkanethiol molecule, which covalently binds to the crystal surface through the thiol group. As expected, heparin sulphate binding growth factors bound to the octasaccharide, but the change in mass of growth factor bound per unit change in dissipation is different for the different growth factors. Suggesting that the structures of the various growth factor-octasaccharide complexes are different, therefore, indicates that the change in dissipation can give insights into the structure, orientation and packing of the oligosaccharide-growth factor complexes.