The Conformation of Fibronectin on Self-Assembled Monolayers with Different Surface Composition: An FTIR/ATR Study

Cheng, Shih-Song; Chittur, Krishnan K.; Sukenik, Chaim N.; Culp, Lloyd A.; Lewandowska, Kristine

doi:10.1006/jcis.1994.1018

Cited by 111 publications

(99 citation statements)

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“…EM studies of Fn deposited on carbon films also show a compact structure 18 and freeze-dried Fn from solution imaged in EM appeared with structures similar to the ones seen here. 35 Studies by Cheng et al 36 and Iwamoto et al 37 show some extent of structural changes of Fn adsorbed to hydrophobic surfaces, as investigated with Fourier transform infrared-attenuated total internal reflection 36 and total internal reflected fluorescence. 37 This might be due to rearrangement of the intramolecular structure between adjacent domains, because they are believed to be stabilized by hydrophobic interactions.…”

Section: Hydrophobic Surfacesmentioning

confidence: 98%

Surface‐dependent conformations of human plasma fibronectin adsorbed to silica, mica, and hydrophobic surfaces, studied with use of Atomic Force Microscopy

Bergkvist

Carlsson

Oscarsson

2002

J Biomedical Materials Res

208

255

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Human plasma fibronectin (Fn) is a large flexible protein stabilized by intermolecular ionic interactions forming a compact structure. On altering solution conditions, the structure can revert to a more expanded state, thereby exposing previously hidden domains (e.g., cell-binding sites). Electron microscopy images of Fn air-sprayed onto mica surfaces show elongated protein structures, indicating a surface-induced structural change. This makes it interesting to investigate the influence of surface properties on the structure of adsorbed Fn. We have used intermittent-contact Atomic Force Microscopy to investigate the structure of Fn adsorbed onto mica, silica, and methylated silica surfaces. We observed that on silica surfaces, which is hydrophilic, most (70%) of the molecules had an elongated structure with partial intramolecular chain interactions, compare to molecules adsorbed on hydrophobic, methylated surfaces, where a compact structure predominated (70%). On mica surfaces, both compact and elongated protein structures were observed, with a slight preference for the elongated form (53%). Results show that surface physical properties influence the molecular structure of fibronectin on adsorption, which could provide useful information in understanding surface-induced in vivo responses.

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Section: Hydrophobic Surfacesmentioning

confidence: 98%

Surface‐dependent conformations of human plasma fibronectin adsorbed to silica, mica, and hydrophobic surfaces, studied with use of Atomic Force Microscopy

Bergkvist

Carlsson

Oscarsson

2002

J Biomedical Materials Res

208

255

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show abstract

“…Indeed, protein secondary structural elements, like the a-helix, bsheets and random coil structures, have characteristic absorbance bands in the Amide I region [15][16][17][18]. Because these bands are considerably broad and overlap significantly, the use of deconvolution or second-derivative techniques is required to mathematically enhance the resolution of the spectrum, separating bands that are intrinsically broader than the instrument resolution [19][20][21].…”

Section: Many Other Authors]mentioning

confidence: 99%

Characterization of S-layer proteins of Lactobacillus by FTIR spectroscopy and differential scanning calorimetry

Mobili

Londero

Maria

et al. 2009

Vibrational Spectroscopy

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“…The conformation of FN has been shown to have a significant effect on cell adhesion. [39,40] From the current data, it is difficult to discern the relative contribution of these two factors in deciding cell adhesion. It is worth noting that while the gradient substrate affords variation of surface properties when viewed over the entire substrate, it also provides areas of homogeneous properties, upon zooming in on a small region of the substrate (areas of the order of hundreds of micrometer squared in our case).…”

mentioning

confidence: 94%

Tailoring Cell Adhesion Using Surface‐Grafted Polymer Gradient Assemblies

et al. 2005

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dominant bandgap emission at 310 nm, along with several higher-energy emissions due to impurity phases.In conclusion, well-defined [ZnSe](DETA) 0.5 nanobelts have been synthesized successfully by tuning the composition of a ternary solution made of DETA, hydrazine hydrate, and deionized water. We find that an appropriate amount of hydrazine hydrate is essential for the formation of elegant [ZnSe](DETA) 0.5 nanobelts. While the optical properties of the nanobelts are not changed significantly, the ability to make these II-VI-based hybrid semiconductor nanostructure microparticles into nanocrystals with uniform shape and size is one step further towards the miniaturization of devices. In addition, surface modification or combination with other materials may introduce new phenomena and properties into this system with remarkable quantum size effects and expand their potential for applications in advanced semiconductor devices. ExperimentalAll chemicals were of analytical grade and used as received without further purification. In a typical procedure, ZnSO 4 ·7H 2 O (0.05 mmol) and Na 2 SeO 3 (0.05 mmol) were added into a mixed solution (35 mL) with a volume ratio of V N 2 H 4 ·H 2 O /V DETA /V H 2 O = 5:14:16 under stirring. The mixed solution was then transferred into a Teflon-lined autoclave (with a filling ratio of 80 %). The autoclave was closed and kept at 180°C for 12 h, and then cooled to room temperature naturally. The white floccules formed after the reaction were washed with distilled water and absolute ethanol, and dried under vacuum at 80°C for 6 h.XRD patterns of the products were obtained on a Japan Rigaku DMax-cA rotation anode X-ray diffractometer equipped with graphite monochromatized Cu Ka radiation (k = 1.54178 Å). TEM images were acquired on a Hitachi Model H-800 instrument at an accelerating voltage of 200 kV. UV-vis spectra were recorded on a Shimadzu UV-240 spectrophotometer at room temperature. PL spectra were measured on a Fluorolog3-TAU-P instrument at room temperature.

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The Conformation of Fibronectin on Self-Assembled Monolayers with Different Surface Composition: An FTIR/ATR Study

Cited by 111 publications

References 0 publications

Surface‐dependent conformations of human plasma fibronectin adsorbed to silica, mica, and hydrophobic surfaces, studied with use of Atomic Force Microscopy

Surface‐dependent conformations of human plasma fibronectin adsorbed to silica, mica, and hydrophobic surfaces, studied with use of Atomic Force Microscopy

Characterization of S-layer proteins of Lactobacillus by FTIR spectroscopy and differential scanning calorimetry

Tailoring Cell Adhesion Using Surface‐Grafted Polymer Gradient Assemblies

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