A novel approach to the preparation of ultra-flat Nickel 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 sub-monolayers. Protein sample exposure to imidazole causes removal of the adsorbates, confirming the involvement of the poly-histidine tail in protein surface immobilization.
Ultraflat Nickel Substrates for Scanning Probe Microscopy of Polyhistidine-Tagged Proteins / Alessandrini, Andrea; Bortolotti, Carlo Augusto; G., Bertoni; A., Vezzoli; P., Facci. - In: JOURNAL OF PHYSICAL CHEMISTRY. C. - ISSN 1932-7447. - STAMPA. - 112:10(2008), pp. 3747-3750. [10.1021/jp0771623]
Ultraflat Nickel Substrates for Scanning Probe Microscopy of Polyhistidine-Tagged Proteins
ALESSANDRINI, Andrea;BORTOLOTTI, Carlo Augusto;
2008
Abstract
A novel approach to the preparation of ultra-flat Nickel 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 sub-monolayers. Protein sample exposure to imidazole causes removal of the adsorbates, confirming the involvement of the poly-histidine tail in protein surface immobilization.
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