Thomas F. Keller
University of Jena
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Publication
Featured researches published by Thomas F. Keller.
ACS Nano | 2011
Thomas F. Keller; Jörg Schönfelder; Jörg Reichert; Nunzio Tuccitto; Antonino Licciardello; Grazia M. L. Messina; Giovanni Marletta; Klaus D. Jandt
Protein adsorption plays a key role in the biological response to implants. We report how nanoscale topography, chemistry, crystallinity, and molecular chain anisotropy of ultrahigh molecular weight polyethylene (UHMWPE) surfaces affect the protein assembly and induce lateral orientational order. We applied ultraflat, melt drawn UHMWPE films to show that highly oriented nanocrystalline lamellae influence the conformation and aggregation into network structures of human plasma fibrinogen by atomic force microscopy with unprecedented clarity and molecular resolution. We observed a transition from random protein orientation at low concentrations to an assembly guided by the UHMWPE surface nanotopography at a close to full surface coverage on hydrophobic melt drawn UHMWPE. This assembly differs from the arrangement at a hydrophobic, on the nanoscale smooth UHMWPE reference. On plasma-modified, hydrophilic melt drawn UHMWPE surfaces that retained their original nanotopography, the influence of the nanoscale surface pattern on the protein adsorption is lost. A model based on protein-surface and protein-protein interactions is proposed. We suggest these nanostructured polymer films to be versatile model surfaces to provide unique information on protein interactions with nanoscale building blocks of implants, such as nanocrystalline UHMWPE lamellae. The current study contributes to the understanding of molecular processes at polymer biointerfaces and may support their future design and molecular scale tailoring.
Chemsuschem | 2009
Christine Schmöger; Achim Stolle; Werner Bonrath; Bernd Ondruschka; Thomas F. Keller; Klaus D. Jandt
A Pd on porous glass catalyst system was used in the liquid-phase hydrogenation of terpenoid substrates with dihydrogen at room temperature and atmospheric pressure. A multitude of substances were hydrogenated selectively with yields of 90-100 %. In all experiments, only C--C, C--N, and N--N double bonds were hydrogenated. Studies revealed that carbonyl and aromatic double bonds are inert towards catalytic reduction with dihydrogen under the conditions employed. In some cases, hydrogenation was accompanied by isomerization, so that treatment of beta-pinene, for example, afforded isomeric alpha-pinene, which was subsequently hydrogenated to pinane.
Langmuir | 2012
Giovanni Li Destri; Thomas F. Keller; Marinella Catellani; Francesco Punzo; Klaus D. Jandt; Giovanni Marletta
The nanostructure of thermally annealed thin films of poly(3-hexylthiophene) (P3HT) and [6,6]-phenyl-C61-butyric acid methyl ester (PCBM) blends on hydrophobic and hydrophilic substrates was studied to unravel the relationship between the substrate properties and the phase structure of polymer blends in confined geometry. Indeed, the nature of the employed substrates was found to affect the extent of phase separation, the PCBM aggregation state and the texture of the whole system. In particular, annealing below the melting temperature of the polymer yielded the formation of PCBM nanometric crystallites on the hydrophobic substrates, while mostly amorphous microscopic aggregates were formed on the hydrophilic ones. Moreover, while an enhanced in-plane orientation of P3HT lamellae was promoted on hydrophobic substrates, a markedly tilted geometry was produced on the hydrophilic ones. The observed effects were interpreted in terms of a simple model connecting the interface free energy for the blend films to the different polymer chain mobility and diffusion velocity of PCBM molecules on the different substrates.
Macromolecular Bioscience | 2010
Daniel Siegismund; Thomas F. Keller; Klaus D. Jandt; Markus Rettenmayr
A model for the adsorption of fibrinogen or, in general, non-globular shaped proteins on solid surfaces are presented. Two-dimensional cellular automata simulations of the adsorption of fibrinogen on two different surfaces were performed. The model includes mass transfer toward the surface, adsorption of fibrinogen molecules, and surface diffusion mechanisms for both fibrinogen molecules and clusters. We show that the major physical processes are represented in the recent model. Particularly, the influence of the surface hydrophobicity on the behavior of fibrinogen. Atomic force microscopy images of fibrinogen adsorption on Si model surfaces with different hydrophobicity are compared to the results.
Langmuir | 2010
Thomas F. Keller; Martin Müller; Wuye Ouyang; Jian-Tao Zhang; Klaus D. Jandt
We report a templating effect of uniaxially oriented melt-drawn polyethylene (MD-PE) films on α-helical poly(L-lysine)/poly(styrenesulfonate) (α-PLL/PSS) complexes deposited by the layer-by-layer (LBL) method. The melt-drawing process induced an MD-PE fiber texture consisting of nanoscale lamellar crystals embedded in amorphous regions on the MD-PE film surface whereby the common crystallographic c axis is the PE molecular chain direction parallel to the uniaxial melt-drawing direction. The MD-PE film and the α-PLL/PSS deposit were analyzed by atomic force microscopy (AFM) and in situ attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR) using polarized light as a complementary method. Both methods revealed that α-PLL/PSS complexes adsorbed at the MD-PE surface were anisotropic and preferentially oriented perpendicular to the crystallographic c direction of the MD-PE film. Quantitatively, from AFM image analysis and ATR-FTIR dichroism of the amide II band of the α-PLL, mean cone opening angles of 12-18° for both rodlike α-PLL and the anisotropic α-PLL/PSS complexes with respect to the PE lamellae width direction were obtained. A model for the preferred alignment of α-PLL along the protruding PE lamellae is discussed, which is based on possible hydrophobic driving forces for the minimization of surface free energy at molecular and supermolecular topographic steps of the PE surface followed by electrostatic interactions between the interconnecting PSS and the α-PLL during layer-by-layer adsorption. This study elucidates the requirements and mechanisms involved in orienting biomolecules and may open up a path for designing templates to induce directed protein adsorption and cell growth by oriented polypeptide- or protein-modified PE surfaces.
Biointerphases | 2012
Jana Sommerfeld; Jessica Richter; Raphael Niepelt; Stefanie Kosan; Thomas F. Keller; Klaus D. Jandt; Carsten Ronning
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 nano-sized morphology while not modifying the stoichiometry/chemistry.
Chinese Journal of Catalysis | 2011
Achim Stolle; Christine Schmöger; Bernd Ondruschka; Werner Bonrath; Thomas F. Keller; Klaus D. Jandt
Abstract Innovative catalysts based on a “porous glass” support material were developed and investigated for the reduction of benzalacetophenone. The easy preparation conditions and possibility to use different metals (e.g. Pd, Pt, Rh) for impregnation gave a broad variety of these catalysts. Hydrogenation experiments with these supported catalysts were carried out under different hydrogen pressures and temperatures. Porous glass catalysts with Pd as the active component gave chemoselective hydrogenation of benzalacetophenone, while Pt- and Rh-catalysts tended to further reduce the carbonyl group, especially at elevated hydrogen pressures and temperatures. Kinetic analysis of the reactions revealed these had zero order kinetics, which was independent of the type of porous glass support and solvent used.
Soft Matter | 2011
Gang Wei; Thomas F. Keller; Jian-Tao Zhang; Klaus D. Jandt
Protein nanofibers (PNFs) created by controlling the self-assembly of protein molecules are contemporary biomacromolecular precursors to construct novel functional nanomaterials. We report here on a facile approach to prepare PNF-based biophotonic nanohybrids. For the first time we demonstrate the creation of fibronectin (FN) nanofibers in highly concentrated ethanol solution and subsequently present the organization of N-hydroxysulfosuccinimide (NHS) modified CdSe–ZnS core–shell quantum dots (QDs) on the self-assembled FN nanofibers by covalent interaction. AFM and TEM results indicate that the formation of FN nanofibers is controllable and the created FN nanofibers are uniform in diameter and length. UV-vis and XPS data identified the successful modification of QDs. The one-dimensional (1-D) PNF–QD biophotonic nanohybrids created by organizing QDs onto FN nanofibers were imaged with AFM, TEM, and confocal laser scanning microscopy, and the results show that the created FN nanofibers can serve as feasible templates to organize QDs for construction of biophotonic nanohybrids. The PNF–QD nanohybrids have potential applications in optical, biomedical and nanotechnological fields.
RSC Advances | 2014
Xiaoyuan Zhang; Zhaofei Ouyang; Robert Schulze; Thomas F. Keller; Klaus D. Jandt; Zhiqiang Su
Various microstructures and phase morphologies of an amphiphilic poly(ethylene oxide)-block-polyethylene (PEO-b-PE) co-oligomer, controlled by topological restriction of PE segments on the tethered PEO chains, were characterized by differential scanning calorimetry (DSC), polarized optical microscopy (POM), scanning electron microscopy (SEM), and synchrotron radiation wide-angle/small-angle X-ray scattering (WAXS/SAXS) in drop-cast films. The crystallization processes were mediated by two pathways, a one-step crystallization process (I) and a sequential crystallization process (II). Results show that the thermal procedures have great influence on the microstructures and phase morphologies of PEO-b-PE co-oligomer, e.g., negative spherulites with radial stripes were detected in the one-step crystallization process (I), while crystalline texture, which contains a large number of crystals with reduced sizes, formed in the sequential crystallization process (II). Based on our experimental data, the topological restriction effect encountered by PEO chains depends on the hard confinement of PE crystals and the soft confinement of amorphous PE in the two crystallization procedures. The formation mechanisms of the long-range order structures within the co-oligomer were elucidated through morphology models. These nano-patterned structures make the double crystalline block copolymers outstanding candidates for surface modification, micromolding, and optoelectronic devices in nanotechnological and biomedical applications.
Acta Biomaterialia | 2013
Thomas F. Keller; Jörg Reichert; Tam Pham Thanh; Ranko Adjiski; Lothar Spiess; Liga Berzina-Cimdina; Klaus D. Jandt; Jörg Bossert
One key for the successful integration of implants into the human body is the control of protein adsorption by adjusting the surface properties at different length scales. This is particularly important for titanium oxide, one of the most common biomedical interfaces. As for titania (TiO(2)) the interface is largely defined by its crystal surface structure, it is crucial to understand how the surface crystallinity affects the structure, properties and function of protein layers mediating subsequent biological reactions. For rutile TiO(2) we demonstrate that the conformation and relative amount of human plasma fibrinogen (HPF) and the structure of adsorbed HPF layers depend on the crystal surface nanostructure by employing thermally etched multi-faceted TiO(2) surfaces. Thermal etching of polycrystalline TiO(2) facilitates a nanoscale crystal faceting and, thus, the creation of different surface nanostructures on a single specimen surface. Atomic force microscopy shows that HPF arranges into networks and thin globular layers on flat and irregular crystal grain surfaces, respectively. On a third, faceted category we observed an alternating conformation of HPF on neighboring facets. The bulk grain orientation obtained from electron backscatter diffraction and thermodynamic mechanisms of surface reconstruction during thermal etching suggest that the grain and facet surface-specific arrangement and relative amount of adsorbed proteins depend on the associated free crystal surface energy. The implications for potentially favorable TiO(2) crystal facets regarding the inflammatory response and hemostasis are discussed with a view to the advanced surface design of future implants.