Ultraflat nickel substrates for scanning probe microscopy of polyhistidine-tagged proteins

被引：9

作者：

Alessandrini, Andrea ^{[1
,2
]}

Bortolotti, Carlo Augusto ^{[1
]}

Bertoni, Giovanni ^{[3
]}

Vezzoli, Alessandro ^{[3
]}

Facci, Paolo ^{[1
]}

机构：

[1] CNR, INFM, Natl Res Ctr Nanostruct & BioSyst Surfaces S3, I-41100 Modena, Italy

[2] Univ Modena & Reggio Emilia, Dept Phys, I-41100 Modena, Italy

[3] Univ Milan, Dept Biomol Sci & Biotechnol, I-20133 Milan, Italy

来源：

JOURNAL OF PHYSICAL CHEMISTRY C | 2008年 / 112卷 / 10期

关键词：

D O I：

10.1021/jp0771623

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 [物理化学]; 081704 [应用化学];

摘要：

A novel approach to the preparation of ultraflat Ni substrates suitable to scanning probe microscopy imaging of immobilized polyhistidine-tagged proteins has been devised. Exploiting freshly cleaved mica, Ni thermal evaporation followed by thermal annealing in vacuum, and the template stripping method, we have obtained Ni substrates with a rms roughness as low as 0.12 nm, which bind readily polyhistidine-tagged proteins, enabling molecular resolution imaging of isolated molecules as well as of molecular submonolayers. Protein sample exposure to imidazole causes removal of the adsorbates, confirming the involvement of the polyhistidine tail in protein surface immobilization.

引用

页码：3747 / 3750

页数：4

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