Ni(ii)-modified solid substrates as a platform to adsorb His-tag proteins

Tuning protein delivery from different architectures of layer-by-layer assemblies on polymer films

“…Before use, the quartz crystals were thoroughly cleaned to remove any organic contaminants present, according to a procedure described elsewhere. 21,22 20 80 AE 1 9 3 AE 11 (Si/SiO 2 /PEI)(Hep/Chi + LYS) 20 70 AE 1 8 3 AE 6 (Si/SiO 2 /PEI)(Hep/Chi) 10 34 AE 5 3 4 AE 2 (Si/SiO 2 /PEI)(Hep + BSA/Chi) 10 29 AE 3 4 0 AE 2 (Si/SiO 2 /PEI)(Hep/Chi + LYS) 10 39…”

“…The changes in resonance frequency (Df n ) and dissipation (DD n ), where n denotes the fundamental tone recorded from the 5th to the 13th overtones, were simultaneously monitored as a function of time. For acoustically rigid films, the mass variation can be calculated from the resonance frequency variation, as described in Sauerbrey's equation (eqn (2)): 21,22 Df…”

An integrated experimental-theoretical approach to understand the electron transfer mechanism of adsorbed ferrocene-terminated alkanethiol monolayers

“…shows the voltammograms of FcC6SH modified Au(111) substrates performed in different electrolytes and scan rates whereas Figure 4 presents the respective M A N U S C R I P T A C C E P T E D ACCEPTED MANUSCRIPTrelationship between the peak current density and the scan rate. Considering that this substrate modification can be coupled to a bioelectrochemical device to improve its performance[12][13][14][15][16], the selected supporting electrolytes represent gradual modifications from the commonly used 1.00 M HClO 4 pH 0.2 in electrochemical determinations to the 0.10 M phosphate buffer (PB) pH 8.5, compatible with surface bioactivity[69][70][71].Clearly, the shape of the voltammograms measured in 1.00 M HClO 4 does not depend on the scan rate. Thus, the FcC6SH monolayer, although heterogeneous, is stable against successive changes of the scan rate in the same electrolyte after the cycling pretreatment.…”

Investigating organic multilayers by spectroscopic ellipsometry: specific and non-specific interactions of polyhistidine with NTA self-assembled monolayers

“…After seminal works [ 3 ], the interaction of chelated Ni ions with oligohistidine peptides has been largely implemented over the years for the affinity purification of recombinant proteins [ 4 – 6 ], and for the development of bioanalytical surfaces [ 7 – 12 ]. To this purpose, self-assembled monolayers (SAMs) terminated with the nitriloacetic acid (NTA) group, after loading with nickel ions (Ni(II)), provide platforms able to specifically bind his-tag proteins [ 13 – 18 ] and enzymes that retain their activity upon immobilization [ 19 – 21 ].…”