J. Heyrovský Institute of Physical Chemistry of ASCR, Prague, Czech Republic.
Biointerphases. 2011 Dec;6(4):164-70. doi: 10.1116/1.3650300.
Nanobubbles formed on monocrystalline gold/water interface by means of the ethanol-to-water solvent exchange were exposed to the solutions of either bovine serum albumin or papain proteins. Both proteins do not change the position of nanobubbles in water, as observed by in situ tapping mode atomic force microscopy imaging before and after the introduction of the protein. The aqueous environment was subsequently replaced by ethanol. While all nanobubbles were found to dissolve in ethanol in the presence of bovine serum albumin, most of them survived when papain was employed. The protective ability of papain was ascribed to its resistance towards the protein denaturation in aqueous solutions of ethanol. The authors employed in situ atomic force nanolithography to investigate the nanomorphology of the papain/nanobubble assemblies in ethanol.
通过乙醇向水的溶剂交换，在单晶金/水界面上形成了纳米气泡，然后将这些纳米气泡暴露于牛血清白蛋白或木瓜蛋白酶蛋白的溶液中。通过原位敲击模式原子力显微镜成像，在引入蛋白质前后观察到，这两种蛋白质都不会改变纳米气泡在水中的位置。随后，将水相环境替换为乙醇。虽然在存在牛血清白蛋白的情况下，所有纳米气泡都被发现溶解在乙醇中，但当使用木瓜蛋白酶时，它们中的大多数都存活了下来。木瓜蛋白酶的保护能力归因于其在乙醇水溶液中对蛋白质变性的抵抗能力。作者使用原位原子力纳米光刻技术研究了乙醇中木瓜蛋白酶/纳米气泡组装体的纳米形态。
