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通过原子力显微镜观察二维晶格蛋白表面上细菌的微图案化。

Micropatterning of bacteria on two-dimensional lattice protein surface observed by atomic force microscopy.

作者信息

Oh Y J, Jo W, Lim J, Park S, Kim Y S, Kim Y

机构信息

Department of Physics and Division of Nano Sciences, Ewha Womans University, Seoul 120-750, Republic of Korea.

出版信息

Ultramicroscopy. 2008 Sep;108(10):1124-7. doi: 10.1016/j.ultramic.2008.04.055. Epub 2008 May 14.

Abstract

In this study, we characterized the two-dimensional lattice of bovine serum albumin (BSA) as a chemical and physical barrier against bacterial adhesion, using fluorescence microscopy and atomic force microscopy (AFM). The lattice of BSA on glass surface was fabricated by micro-contact printing (microCP), which is a useful way to pattern a wide range of molecules into microscale features on different types of substrates. The contact-mode AFM measurements showed that the average height of the printed BSA monolayer was 5-6 nm. Escherichia coli adhered rapidly on bare glass slide, while the bacterial adhesion was minimized on the lattices in the range of 1-3 microm(2). Especially, the bacterial adhesion was completely inhibited on a 1 microm(2) lattice. The results suggest that the anti-adhesion effects are due by the steric repulsion forces exerted by BSA.

摘要

在本研究中,我们利用荧光显微镜和原子力显微镜(AFM),将牛血清白蛋白(BSA)的二维晶格表征为一种防止细菌粘附的化学和物理屏障。玻璃表面的BSA晶格通过微接触印刷(microCP)制备,这是一种将各种分子图案化为不同类型基板上微尺度特征的有用方法。接触模式原子力显微镜测量表明,印刷的BSA单层的平均高度为5 - 6纳米。大肠杆菌在裸露的载玻片上迅速粘附,而在1 - 3微米²范围内的晶格上细菌粘附最小化。特别是,在1微米²的晶格上细菌粘附被完全抑制。结果表明,抗粘附作用是由BSA施加的空间排斥力所致。

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