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Self‐assembly and recrystallization of bacterial S‐layer proteins at silicon supports imaged in real time by atomic force microscopy
Author(s) -
Györvary E. S.,
Stein O.,
Pum D.,
Sleytr U. B.
Publication year - 2003
Publication title -
journal of microscopy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.569
H-Index - 111
eISSN - 1365-2818
pISSN - 0022-2720
DOI - 10.1111/j.1365-2818.2003.01270.x
Subject(s) - s layer , silicon , monolayer , wafer , chemistry , bilayer , crystallography , layer (electronics) , atomic force microscopy , ionic bonding , chemical engineering , materials science , nanotechnology , membrane , ion , organic chemistry , biochemistry , engineering , gene
Summary The self‐assembly of bacterial surface‐layer (S‐layer) proteins (SbpA of Bacillus sphaericus CCM 2177) at silicon supports (hydrophobic, non‐plasma‐treated and hydrophilic, O 2 plasma‐treated silicon supports) was imaged in real time by atomic force microscopy (AFM). A closed mosaic layer consisting of small crystals (less than 200 nm in diameter) was formed at a hydrophobic silicon support, whereas a coherent crystalline lattice consisting of large domains (2–10 µm in size) was generated at O 2 plasma‐treated, hydrophilic silicon wafers. The structure of the formed layers was a monolayer (9 nm in height) at the hydrophobic silicon and a bilayer (15 nm in height) at the hydrophilic silicon. In situ AFM measurements confirmed the importance of ionic bonds in the formation of crystalline SbpA layers at silicon supports. Rupture of the protein subunits with a metal chelator from the crystalline lattice of SbpA was visualized in situ by AFM. The stability of solid‐supported SbpA layers could be enhanced by cross‐linking the S‐layers with amino–amino or amino–carboxyl group directed cross‐linkers.