Details
| Originalsprache | Englisch |
|---|---|
| Aufsatznummer | 55 |
| Seiten (von - bis) | 1-7 |
| Seitenumfang | 7 |
| Fachzeitschrift | BIOINTERPHASES |
| Jahrgang | 7 |
| Ausgabenummer | 1-4 |
| Publikationsstatus | Veröffentlicht - 2012 |
| Extern publiziert | Ja |
Abstract
We synthesized nano-scaled periodic ripple patterns on silicon and titanium dioxide (TiO2) surfaces by xenon ion irradiation, and performed adsorption experiments with human plasma fibrinogen (HPF) on such surfaces as a function of the ripple wavelength. Atomic force microscopy showed the adsorption of HPF in mostly globular conformation on crystalline and amorphous flat Si surfaces as well as on nano-structured Si with long ripple wavelengths. For short ripple wavelengths the proteins seem to adsorb in a stretched formation and align across or along the ripples. In contrast to that, the proteins adsorb in a globular assembly on flat and long-wavelength rippled TiO2, but no adsorbed proteins could be observed on TiO2 with short ripple wavelengths due to a decrease of the adsorption energy caused by surface curvature. Consequently, the adsorption behavior of HPF can be tuned on biomedically interesting materials by introducing a nanosized morphology while not modifying the stoichiometry/ chemistry.
ASJC Scopus Sachgebiete
- Chemie (insg.)
- Allgemeine Chemie
- Werkstoffwissenschaften (insg.)
- Biomaterialien
- Werkstoffwissenschaften (insg.)
- Allgemeine Materialwissenschaften
- Biochemie, Genetik und Molekularbiologie (insg.)
- Allgemeine Biochemie, Genetik und Molekularbiologie
- Physik und Astronomie (insg.)
- Allgemeine Physik und Astronomie
Zitieren
- Standard
- Harvard
- Apa
- Vancouver
- BibTex
- RIS
in: BIOINTERPHASES, Jahrgang 7, Nr. 1-4, 55, 2012, S. 1-7.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Protein adsorption on nano-scaled, rippled TiO2 and Si surfaces
AU - Sommerfeld, Jana
AU - Richter, Jessica
AU - Niepelt, Raphael
AU - Kosan, Stefanie
AU - Keller, Thomas F.
AU - Jandt, Klaus D.
AU - Ronning, Carsten
PY - 2012
Y1 - 2012
N2 - We synthesized nano-scaled periodic ripple patterns on silicon and titanium dioxide (TiO2) surfaces by xenon ion irradiation, and performed adsorption experiments with human plasma fibrinogen (HPF) on such surfaces as a function of the ripple wavelength. Atomic force microscopy showed the adsorption of HPF in mostly globular conformation on crystalline and amorphous flat Si surfaces as well as on nano-structured Si with long ripple wavelengths. For short ripple wavelengths the proteins seem to adsorb in a stretched formation and align across or along the ripples. In contrast to that, the proteins adsorb in a globular assembly on flat and long-wavelength rippled TiO2, but no adsorbed proteins could be observed on TiO2 with short ripple wavelengths due to a decrease of the adsorption energy caused by surface curvature. Consequently, the adsorption behavior of HPF can be tuned on biomedically interesting materials by introducing a nanosized morphology while not modifying the stoichiometry/ chemistry.
AB - We synthesized nano-scaled periodic ripple patterns on silicon and titanium dioxide (TiO2) surfaces by xenon ion irradiation, and performed adsorption experiments with human plasma fibrinogen (HPF) on such surfaces as a function of the ripple wavelength. Atomic force microscopy showed the adsorption of HPF in mostly globular conformation on crystalline and amorphous flat Si surfaces as well as on nano-structured Si with long ripple wavelengths. For short ripple wavelengths the proteins seem to adsorb in a stretched formation and align across or along the ripples. In contrast to that, the proteins adsorb in a globular assembly on flat and long-wavelength rippled TiO2, but no adsorbed proteins could be observed on TiO2 with short ripple wavelengths due to a decrease of the adsorption energy caused by surface curvature. Consequently, the adsorption behavior of HPF can be tuned on biomedically interesting materials by introducing a nanosized morphology while not modifying the stoichiometry/ chemistry.
UR - http://www.scopus.com/inward/record.url?scp=84871127011&partnerID=8YFLogxK
U2 - 10.1007/s13758-012-0055-5
DO - 10.1007/s13758-012-0055-5
M3 - Article
C2 - 22956465
AN - SCOPUS:84871127011
VL - 7
SP - 1
EP - 7
JO - BIOINTERPHASES
JF - BIOINTERPHASES
SN - 1934-8630
IS - 1-4
M1 - 55
ER -