Recognition imaging and highly ordered molecular templating of bacterial S-layer nanoarrays containing affinity-tags.
Functional nanoarrays were fabricated using the chimeric bacterial cell surface layer (S-layer) protein rSbpA fused with the affinity tag Strep-tagII and characterized using various atomic force microscopy (AFM) techniques in aqueous environment. The accessibility of Strep-tagII was verified by single-molecule force spectroscopy studies employing Strep-Tactin as specific ligand. Simultaneous topography and recognition imaging (TREC) of the nanoarray yielded high resolution maps of the Strep-tagll binding sites with a positional accuracy of 1.5 nm. The nanoarrays were used as template for constructing highly ordered molecular binding blocks.
Institute of Biophysics, Johannes Kepler University of Linz, 4040 Linz, Austria.
Jilin
J
Tang
Andreas
A
Ebner
Helga
H
Badelt-Lichtblau
Christine
C
Völlenkle
Christian
C
Rankl
Bernhard
B
Kraxberger
Michael
M
Leitner
Linda
L
Wildling
Hermann J
HJ
Gruber
Uwe B
UB
Sleytr
Nicola
N
Ilk
Peter
P
Hinterdorfer
D000345:Affinity Labels; D001419:Bacteria / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D001483:Base Sequence; D003460:Crystallization; D017931:DNA Primers; D018625:Microscopy, Atomic Force; D009004:Monosaccharide Transport Proteins / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry
D000345:Affinity Labels; C099517:Ala-Trp-Arg-His-Pro-Gln-Phe-Gly-Gly; D001426:Bacterial Proteins; D017931:DNA Primers; D009004:Monosaccharide Transport Proteins; D009842:Oligopeptides; D011994:Recombinant Proteins; C120455:SbpA protein, bacteria