Abstract
In this study, we present the scanning force and electron microscopic visualization of single molecules of fibronectin either frozen hydrated or adsorbed onto metallic and polymeric surfaces with different solid surface tensions. The surfaces were characterized by dynamic contact angle measurements, X-ray photo emission spectroscopy (XPS or ESCA) and scanning force microscopy. The proteins were prepared by fast protein liquid chromatography (FPLC) and characterized by gel electrophoresis. Protein films on surfaces were investigated by surface plasmon resonance spectroscopy and directly imaged by scanning force microscopy. The spreading of the adsorbed fibronectin revealed dependence on the chemical composition and the solid surface tension. Structure of fibronectin in solution as well as on solid interface appeared as an extended straight strand as obtained by imaging with electron and scanning probe microscopies. Imaging of DNA was performed by scanning force microscopy to test the accuracy and reproducibility of our measurements. The measured contour lengths were accurate and the larger widths were caused by convolution of the tip shape and sample. Frictional forces during the scan have been of significant contribution in the imaging mechanism. Moreover, this work demonstrated that scanning force microscopy can be used for mapping the orientation and organization of protein film adsorbed onto various surfaces at the nanoscale.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 378-388 |
| Number of pages | 11 |
| Journal | Journal of Electron Microscopy |
| Volume | 42 |
| Issue number | 6 |
| State | Published - Dec 1993 |
| Externally published | Yes |
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Keywords
- Adsorption
- Cryo TEM
- Fibronectin
- Scanning probe techniques (SPM)
ASJC Scopus subject areas
- Statistics, Probability and Uncertainty
- Applied Mathematics
- Physiology (medical)
- Infectious Diseases
- Pharmacology (medical)
- Instrumentation
Cite this
Solution structure and direct imaging of fibronectin adsorption to solid surfaces by scanning force microscopy and cryo-electron microscopy. / Zenhausern, Frederic; Adrian, Marc; Descouts, P.
In: Journal of Electron Microscopy, Vol. 42, No. 6, 12.1993, p. 378-388.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Solution structure and direct imaging of fibronectin adsorption to solid surfaces by scanning force microscopy and cryo-electron microscopy
AU - Zenhausern, Frederic
AU - Adrian, Marc
AU - Descouts, P.
PY - 1993/12
Y1 - 1993/12
N2 - In this study, we present the scanning force and electron microscopic visualization of single molecules of fibronectin either frozen hydrated or adsorbed onto metallic and polymeric surfaces with different solid surface tensions. The surfaces were characterized by dynamic contact angle measurements, X-ray photo emission spectroscopy (XPS or ESCA) and scanning force microscopy. The proteins were prepared by fast protein liquid chromatography (FPLC) and characterized by gel electrophoresis. Protein films on surfaces were investigated by surface plasmon resonance spectroscopy and directly imaged by scanning force microscopy. The spreading of the adsorbed fibronectin revealed dependence on the chemical composition and the solid surface tension. Structure of fibronectin in solution as well as on solid interface appeared as an extended straight strand as obtained by imaging with electron and scanning probe microscopies. Imaging of DNA was performed by scanning force microscopy to test the accuracy and reproducibility of our measurements. The measured contour lengths were accurate and the larger widths were caused by convolution of the tip shape and sample. Frictional forces during the scan have been of significant contribution in the imaging mechanism. Moreover, this work demonstrated that scanning force microscopy can be used for mapping the orientation and organization of protein film adsorbed onto various surfaces at the nanoscale.
AB - In this study, we present the scanning force and electron microscopic visualization of single molecules of fibronectin either frozen hydrated or adsorbed onto metallic and polymeric surfaces with different solid surface tensions. The surfaces were characterized by dynamic contact angle measurements, X-ray photo emission spectroscopy (XPS or ESCA) and scanning force microscopy. The proteins were prepared by fast protein liquid chromatography (FPLC) and characterized by gel electrophoresis. Protein films on surfaces were investigated by surface plasmon resonance spectroscopy and directly imaged by scanning force microscopy. The spreading of the adsorbed fibronectin revealed dependence on the chemical composition and the solid surface tension. Structure of fibronectin in solution as well as on solid interface appeared as an extended straight strand as obtained by imaging with electron and scanning probe microscopies. Imaging of DNA was performed by scanning force microscopy to test the accuracy and reproducibility of our measurements. The measured contour lengths were accurate and the larger widths were caused by convolution of the tip shape and sample. Frictional forces during the scan have been of significant contribution in the imaging mechanism. Moreover, this work demonstrated that scanning force microscopy can be used for mapping the orientation and organization of protein film adsorbed onto various surfaces at the nanoscale.
KW - Adsorption
KW - Cryo TEM
KW - Fibronectin
KW - Scanning probe techniques (SPM)
UR - http://www.scopus.com/inward/record.url?scp=0027830673&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027830673&partnerID=8YFLogxK
M3 - Article
C2 - 8176331
AN - SCOPUS:0027830673
VL - 42
SP - 378
EP - 388
JO - Microscopy (Oxford, England)
JF - Microscopy (Oxford, England)
SN - 2050-5698
IS - 6
ER -