Fusion of purple membranes triggered by immobilization on carbon nanomembranes

• René Riedel,
• Natalie Frese,
• Fang Yang,
• Martin Wortmann,
• Raphael Dalpke,
• Daniel Rhinow,
• Norbert Hampp and
• Armin Gölzhäuser

Beilstein J. Nanotechnol. 2021, 12, 93–101, doi:10.3762/bjnano.12.8

• electron irradiation-induced cross-linking of a self-assembled monolayer (SAM) of 4′-nitro-1,1′-biphenyl-4-thiol (NBPT) and second, purple membrane (PM) containing genetically modified bacteriorhodopsin (BR) carrying a C-terminal His-tag. The NBPT-CNM was further modified to carry nitrilotriacetic acid

• (NTA) terminal groups for the interaction with the His-tagged PMs forming a quasi-monolayer of His-tagged PM on top of the CNM-NTA. The formation of the Ni-NTA/His-tag complex leads to the unidirectional orientation of PM on the CNM substrate. Electrophoretic sedimentation was employed to optimize the

• different parameters have been investigated. Fusion first needs uniform orientation. This is accomplished by the His-tag. The lipid composition of the outer and the inner side of the PM differs. In the second step, the recrystallization of the PM patches starts in areas where they were overlapping after

Uptake of the proteins HTRA1 and HTRA2 by cells mediated by calcium phosphate nanoparticles

• Olga Rotan,
• Katharina N. Severin,
• Simon Pöpsel,
• Alexander Peetsch,
• Melisa Merdanovic,
• Michael Ehrmann and
• Matthias Epple

Beilstein J. Nanotechnol. 2017, 8, 381–393, doi:10.3762/bjnano.8.40

• proteins HTRA1 and HTRA2 HTRA1 was produced and purified as described previously [45]. BL21 DE3-Rosetta E. coli cells were used to express HTRA2 with an N-terminal His-tag (pET28a Vector containing codons 134-458 of HTRA2, a kind gift from Antonis S. Zervos, University of Central Florida). HTRA2 expression

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

• Ilaria Solano,
• Pietro Parisse,
• Ornella Cavalleri,
• Federico Gramazio,
• Loredana Casalis and
• Maurizio Canepa

Beilstein J. Nanotechnol. 2016, 7, 544–553, doi:10.3762/bjnano.7.48

• the adsorption of His6 on the Ni-free NTA layer, due to non specific interactions, from the formation of a neatly thicker His6 film induced by the Ni(II)-loading of the NTA SAM. Keywords: His-tag; nitrilotriacetic acid (NTA); protein binding; self-assembled monolayers (SAMs); spectroscopic

• (NTA) group, after loading with nickel ions (Ni(II)), provide platforms able to specifically bind his-tag proteins [13][14][15][16][17][18] and enzymes that retain their activity upon immobilization [19][20][21]. The affinity between the adsorbent surface and the protein can be modulated, e.g., by