Crystalline Bacterial Protein Nanolayers for Cell Micropatterning

Mario Rothbauer; Seta Küpcü; Uwe B. Sleytr; Peter Ertl

doi:10.1007/978-3-319-11128-5_84

Crystalline Bacterial Protein Nanolayers for Cell Micropatterning

Mario Rothbauer
, Seta Küpcü
, Uwe B. Sleytr
, Peter Ertl

University of Natural Resources and Life Sciences Vienna (BOKU)

Research output: Chapter in Book or Conference Proceedings › Conference Proceedings without Presentation › peer-review

Abstract

We have developed a robust cell patterning method using micromolding in capillaries (MIMIC) and self-assembled crystalline bacterial protein (S-layer) monolayers. The unique self-assembly properties of proteins SbpA and SbsB are exploited to create an anisotropic protein nanobiointerface with spatially-defined cytophilic (adhesive) and cytophobic (repulsive) properties. The chosen S-layer proteins were characterized using atomic force microscopy (AFM), zeta-potential and contact angle measurements. Results revealed distinct differences in surface topography and physico-chemical properties between SbsB and SbpA monolayers. Stability testing of cytophobic protein SbpA using vacuum-drying deposition and re-assembly on-flow sowed no remarkable differences with respect to the antifouling properties. Finally, using MIMIC micropatterns of epithelial CaCo-2 cell as well as mobile Jurkat cells were established using anisotropic S-layer protein monolayers

Original language	English
Title of host publication	6th European Conference of the International Federation for Medical and Biological Engineering
Pages	337-340
Number of pages	4
DOIs	https://doi.org/10.1007/978-3-319-11128-5_84
Publication status	Published - 2015

Research Field

Biosensor Technologies

Keywords

micromolding in capillaries; cellular micropatterning; protein self-assembly; S-layer proteins

Access to Document

10.1007/978-3-319-11128-5_84Licence: Unspecified

Cite this

@inbook{47bd636f3cd34a6697eca0b770727949,

title = "Crystalline Bacterial Protein Nanolayers for Cell Micropatterning",

abstract = "We have developed a robust cell patterning method using micromolding in capillaries (MIMIC) and self-assembled crystalline bacterial protein (S-layer) monolayers. The unique self-assembly properties of proteins SbpA and SbsB are exploited to create an anisotropic protein nanobiointerface with spatially-defined cytophilic (adhesive) and cytophobic (repulsive) properties. The chosen S-layer proteins were characterized using atomic force microscopy (AFM), zeta-potential and contact angle measurements. Results revealed distinct differences in surface topography and physico-chemical properties between SbsB and SbpA monolayers. Stability testing of cytophobic protein SbpA using vacuum-drying deposition and re-assembly on-flow sowed no remarkable differences with respect to the antifouling properties. Finally, using MIMIC micropatterns of epithelial CaCo-2 cell as well as mobile Jurkat cells were established using anisotropic S-layer protein monolayers",

keywords = "micromolding in capillaries; cellular micropatterning; protein self-assembly; S-layer proteins, micromolding in capillaries; cellular micropatterning; protein self-assembly; S-layer proteins",

author = "Mario Rothbauer and Seta K{\"u}pc{\"u} and Sleytr, \{Uwe B.\} and Peter Ertl",

year = "2015",

doi = "10.1007/978-3-319-11128-5\_84",

language = "English",

isbn = "978-3-319-11127-8",

pages = "337--340",

booktitle = "6th European Conference of the International Federation for Medical and Biological Engineering",

}

TY - CHAP

T1 - Crystalline Bacterial Protein Nanolayers for Cell Micropatterning

AU - Rothbauer, Mario

AU - Küpcü, Seta

AU - Sleytr, Uwe B.

AU - Ertl, Peter

PY - 2015

Y1 - 2015

N2 - We have developed a robust cell patterning method using micromolding in capillaries (MIMIC) and self-assembled crystalline bacterial protein (S-layer) monolayers. The unique self-assembly properties of proteins SbpA and SbsB are exploited to create an anisotropic protein nanobiointerface with spatially-defined cytophilic (adhesive) and cytophobic (repulsive) properties. The chosen S-layer proteins were characterized using atomic force microscopy (AFM), zeta-potential and contact angle measurements. Results revealed distinct differences in surface topography and physico-chemical properties between SbsB and SbpA monolayers. Stability testing of cytophobic protein SbpA using vacuum-drying deposition and re-assembly on-flow sowed no remarkable differences with respect to the antifouling properties. Finally, using MIMIC micropatterns of epithelial CaCo-2 cell as well as mobile Jurkat cells were established using anisotropic S-layer protein monolayers

AB - We have developed a robust cell patterning method using micromolding in capillaries (MIMIC) and self-assembled crystalline bacterial protein (S-layer) monolayers. The unique self-assembly properties of proteins SbpA and SbsB are exploited to create an anisotropic protein nanobiointerface with spatially-defined cytophilic (adhesive) and cytophobic (repulsive) properties. The chosen S-layer proteins were characterized using atomic force microscopy (AFM), zeta-potential and contact angle measurements. Results revealed distinct differences in surface topography and physico-chemical properties between SbsB and SbpA monolayers. Stability testing of cytophobic protein SbpA using vacuum-drying deposition and re-assembly on-flow sowed no remarkable differences with respect to the antifouling properties. Finally, using MIMIC micropatterns of epithelial CaCo-2 cell as well as mobile Jurkat cells were established using anisotropic S-layer protein monolayers

KW - micromolding in capillaries; cellular micropatterning; protein self-assembly; S-layer proteins

U2 - 10.1007/978-3-319-11128-5_84

DO - 10.1007/978-3-319-11128-5_84

M3 - Conference Proceedings without Presentation

SN - 978-3-319-11127-8

SP - 337

EP - 340

BT - 6th European Conference of the International Federation for Medical and Biological Engineering

ER -

Crystalline Bacterial Protein Nanolayers for Cell Micropatterning

Abstract

Research Field

Keywords

Access to Document

Fingerprint

Cite this