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Sökning: id:"swepub:oai:research.chalmers.se:c684d3c4-2e3e-424c-b84f-0752792ef1b1" > Protein adsorption ...

Protein adsorption on model surfaces with controlled nanotopography and chemistry

Denis, F. A. (författare)
Hanarp, Per, 1974 (författare)
Chalmers tekniska högskola,Chalmers University of Technology
Sutherland, Duncan, 1970 (författare)
Chalmers tekniska högskola,Chalmers University of Technology
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Gold, Julie, 1963 (författare)
Chalmers tekniska högskola,Chalmers University of Technology
Mustin, C. (författare)
Rouxhet, P. G. (författare)
Dufrene, Y. F. (författare)
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 (creator_code:org_t)
2002-01-11
2002
Engelska.
Ingår i: Langmuir. - : American Chemical Society (ACS). - 1520-5827 .- 0743-7463. ; 18:3, s. 819-828
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
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  • To evaluate the influence of substratum surface characteristics on protein adsorption processes, we have investigated the adsorption (adsorbed amount, supramolecular organization) of collagen on model substrata exhibiting controlled topography and surface chemistry. Substrata were prepared in two steps: (i) gold deposition onto silicon wafers (smooth substrata) and onto a support with nanoscale protrusions created by colloidal lithography (rough substrata); (ii) functionalization with CH3 (hydrophobic) and OH (hydrophilic) groups, using alkanethiol self-assembly. Atomic force microscopy (AFM) images were recorded under water, prior to and after collagen adsorption, and the images were analyzed quantitatively using two independent approaches. On smooth substrata, collagen formed a similar to6 nm thick, homogeneous layer with low roughness on hydrophilic surfaces, and a similar to20 nm thick layer exhibiting elongated aggregated structures on hydrophobic surfaces. Film thickness measurements (AFM) together with X-ray photoelectron spectroscopy (XPS) revealed larger adsorbed amounts on hydrophobic surfaces compared to hydrophilic ones. On rough substrata, the adsorbed amounts were similar to those found on smooth substrata; however, the collagen molecules no longer formed aggregated structures on the hydrophobic surfaces. It is concluded that while the adsorbed amount is only affected by the surface chemistry, the supramolecular organization of the adsorbed layer is controlled both by surface chemistry and topography. The approach presented here will have great value in biophysics for investigating bioadsorption and bioadhesion processes on substrata of defined surface properties.

Ämnesord

NATURVETENSKAP  -- Kemi -- Fysikalisk kemi (hsv//swe)
NATURAL SCIENCES  -- Chemical Sciences -- Physical Chemistry (hsv//eng)
TEKNIK OCH TEKNOLOGIER  -- Materialteknik -- Annan materialteknik (hsv//swe)
ENGINEERING AND TECHNOLOGY  -- Materials Engineering -- Other Materials Engineering (hsv//eng)
MEDICIN OCH HÄLSOVETENSKAP  -- Medicinsk bioteknologi -- Biomaterialvetenskap (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Medical Biotechnology -- Biomaterials Science (hsv//eng)

Nyckelord

solid-liquid
immobilization
films
collagen
self-assembled monolayers
atomic-force microscopy
interfaces
conformation
gold
wetting properties
adhesion forces

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