Protein adsorption on topographically nanostructured titanium

C. Galli; M. Collaud Coen; R. Hauert; V. L. Katanaev; M. P. Wymann; P. Gröning; L. Schlapbach

doi:10.1016/S0039-6028(00)01054-2

Protein adsorption on topographically nanostructured titanium

C. Galli^*, M. Collaud Coen, R. Hauert, V. L. Katanaev, M. P. Wymann, P. Gröning, L. Schlapbach

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

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Abstract

We study the protein adsorption on surfaces in order to investigate their predominant role in biocompatibility. Nanostructures are created by local anodic oxidation on titanium using the atomic force microscope. A remarkable specificity of the actin filament adsorption on the nanostructure height is noticed. F-actin is observed to have a low adsorption on nanostructures of a height of 4 nm and the adsorbed proteins appear to be randomly oriented. In contrast high protein adsorption is observed for structure height between 1 and 2 nm, moreover the filaments adsorb preferentially parallel to the nanostructured pattern.

Original language	English
Article number	2773
Pages (from-to)	L180-L184
Journal	Surface Science
Volume	474
Issue number	1-3
DOIs	https://doi.org/10.1016/S0039-6028(00)01054-2
Publication status	Published - 2001
Externally published	Yes

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10.1016/S0039-6028(00)01054-2

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title = "Protein adsorption on topographically nanostructured titanium",

abstract = "We study the protein adsorption on surfaces in order to investigate their predominant role in biocompatibility. Nanostructures are created by local anodic oxidation on titanium using the atomic force microscope. A remarkable specificity of the actin filament adsorption on the nanostructure height is noticed. F-actin is observed to have a low adsorption on nanostructures of a height of 4 nm and the adsorbed proteins appear to be randomly oriented. In contrast high protein adsorption is observed for structure height between 1 and 2 nm, moreover the filaments adsorb preferentially parallel to the nanostructured pattern.",

author = "C. Galli and {Collaud Coen}, M. and R. Hauert and Katanaev, {V. L.} and Wymann, {M. P.} and P. Gr{\"o}ning and L. Schlapbach",

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AU - Galli, C.

AU - Collaud Coen, M.

AU - Hauert, R.

AU - Katanaev, V. L.

AU - Wymann, M. P.

AU - Gröning, P.

AU - Schlapbach, L.

PY - 2001

Y1 - 2001

N2 - We study the protein adsorption on surfaces in order to investigate their predominant role in biocompatibility. Nanostructures are created by local anodic oxidation on titanium using the atomic force microscope. A remarkable specificity of the actin filament adsorption on the nanostructure height is noticed. F-actin is observed to have a low adsorption on nanostructures of a height of 4 nm and the adsorbed proteins appear to be randomly oriented. In contrast high protein adsorption is observed for structure height between 1 and 2 nm, moreover the filaments adsorb preferentially parallel to the nanostructured pattern.

AB - We study the protein adsorption on surfaces in order to investigate their predominant role in biocompatibility. Nanostructures are created by local anodic oxidation on titanium using the atomic force microscope. A remarkable specificity of the actin filament adsorption on the nanostructure height is noticed. F-actin is observed to have a low adsorption on nanostructures of a height of 4 nm and the adsorbed proteins appear to be randomly oriented. In contrast high protein adsorption is observed for structure height between 1 and 2 nm, moreover the filaments adsorb preferentially parallel to the nanostructured pattern.

UR - http://www.scopus.com/inward/record.url?scp=0034826299&partnerID=8YFLogxK

U2 - 10.1016/S0039-6028(00)01054-2

DO - 10.1016/S0039-6028(00)01054-2

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VL - 474

SP - L180-L184

JO - Surface Science

JF - Surface Science

IS - 1-3

M1 - 2773

ER -

Protein adsorption on topographically nanostructured titanium

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