Exploitation of S-layer anisotropy: pH-dependent nanolayer orientation for cellular micropatterning
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Exploitation of S-layer anisotropy : pH-dependent nanolayer orientation for cellular micropatterning. / Rothbauer, Mario; Küpcü, Seta; Sticker, Drago; Sleytr, Uwe B; Ertl, Peter.
In: A C S Nano, Vol. 7, No. 9, 24.09.2013, p. 8020-30.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Exploitation of S-layer anisotropy
T2 - pH-dependent nanolayer orientation for cellular micropatterning
AU - Rothbauer, Mario
AU - Küpcü, Seta
AU - Sticker, Drago
AU - Sleytr, Uwe B
AU - Ertl, Peter
PY - 2013/9/24
Y1 - 2013/9/24
N2 - We have developed a tunable, facile, and reliable cell patterning method using a self-assembled crystalline protein monolayer that, depending on its orientation, can exhibit either cell adhesive (cytophilic) or cell repulsive (cytophobic) surface properties. Our technique exploits, for the first time, the inherent biological anisotropy of the bacterial cell wall protein SbpA capable of interacting with its cytophilic inner side with components of the cell wall, while its outer cytophobic side interacts with the environment. By simply altering the recrystallization protocol from a basic to an acidic condition, the SbpA-protein layer orientation and function can be switched from preventing unspecific protein adsorption and cell adhesion to effectively promote cell attachment, spreading, and proliferation. As a result, the same protein solution can be used to form cell adhesive and repulsive regions over large areas on a single substrate using a simple pH-dependent self-assembly procedure. The reliable establishment of cytophobic and cytophilic SbpA layers allows the generation of well-defined surface patterns that exhibit uniform height (9-10 nm), p4 lattice symmetry with center-to-center spacing of the morphological units of 12 nm, as well as similar surface potential and charge distributions under cell culture conditions. The pH-dependent "orientation switch" of the SbpA protein nanolayer was integrated with micromolding in capillaries (MIMIC) technology to demonstrate its application for cell patterning using a variety of cell lines including epithelial, fibroblast and endothelial cells.
AB - We have developed a tunable, facile, and reliable cell patterning method using a self-assembled crystalline protein monolayer that, depending on its orientation, can exhibit either cell adhesive (cytophilic) or cell repulsive (cytophobic) surface properties. Our technique exploits, for the first time, the inherent biological anisotropy of the bacterial cell wall protein SbpA capable of interacting with its cytophilic inner side with components of the cell wall, while its outer cytophobic side interacts with the environment. By simply altering the recrystallization protocol from a basic to an acidic condition, the SbpA-protein layer orientation and function can be switched from preventing unspecific protein adsorption and cell adhesion to effectively promote cell attachment, spreading, and proliferation. As a result, the same protein solution can be used to form cell adhesive and repulsive regions over large areas on a single substrate using a simple pH-dependent self-assembly procedure. The reliable establishment of cytophobic and cytophilic SbpA layers allows the generation of well-defined surface patterns that exhibit uniform height (9-10 nm), p4 lattice symmetry with center-to-center spacing of the morphological units of 12 nm, as well as similar surface potential and charge distributions under cell culture conditions. The pH-dependent "orientation switch" of the SbpA protein nanolayer was integrated with micromolding in capillaries (MIMIC) technology to demonstrate its application for cell patterning using a variety of cell lines including epithelial, fibroblast and endothelial cells.
KW - Adsorption
KW - Anisotropy
KW - Bacterial Proteins
KW - Caco-2 Cells
KW - Cell Adhesion
KW - Cell Culture Techniques
KW - Cell Separation
KW - Coated Materials, Biocompatible
KW - HeLa Cells
KW - Hep G2 Cells
KW - Humans
KW - Hydrogen-Ion Concentration
KW - Materials Testing
KW - Molecular Conformation
KW - Molecular Imprinting
KW - Monosaccharide Transport Proteins
KW - Nanostructures
KW - Protein Binding
KW - Static Electricity
KW - Surface Properties
KW - Journal Article
KW - Research Support, Non-U.S. Gov't
U2 - 10.1021/nn403198a
DO - 10.1021/nn403198a
M3 - Journal article
C2 - 24004386
VL - 7
SP - 8020
EP - 8030
JO - A C S Nano
JF - A C S Nano
SN - 1936-0851
IS - 9
ER -
ID: 183799724