Solution structure and direct imaging of fibronectin adsorption to solid surfaces by scanning force microscopy and cryo-electron microscopy

Frederic Zenhausern, Marc Adrian, P. Descouts

Research output: Contribution to journalArticle

25 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)378-388
Number of pages11
JournalJournal of Electron Microscopy
Volume42
Issue number6
StatePublished - Dec 1993
Externally publishedYes

Fingerprint

Fibronectin
Cryoelectron Microscopy
Atomic Force Microscopy
Electron Microscopy
Fibronectins
Adsorption
Microscopy
solid surfaces
Electron microscopy
Scanning
Atomic force microscopy
electron microscopy
Imaging
microscopy
Proteins
Imaging techniques
adsorption
Surface Tension
scanning
proteins

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

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AU - Adrian, Marc

AU - Descouts, P.

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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.

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