Janshoff, Andreas

[["dc.bibliographiccitation.firstpage","141"],["dc.bibliographiccitation.lastpage","182"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.editor","Grandin, H. Michelle"],["dc.contributor.editor","Textor, Marcus"],["dc.date.accessioned","2017-09-07T11:54:18Z"],["dc.date.available","2017-09-07T11:54:18Z"],["dc.date.issued","2012"],["dc.identifier.doi","10.1002/9781118181249.ch5"],["dc.identifier.gro","3145143"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2847"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.status","public"],["dc.notes.status","final"],["dc.publisher","Wiley-Blackwell"],["dc.relation.isbn","978-0-470-53650-6"],["dc.relation.ispartof","Intelligent Surfaces in Biotechnology: Scientific and Engineering Concepts, Enabling Technologies, and Translation to Bio-Oriented Applications"],["dc.title","Supported Lipid Bilayers: Intelligent Surfaces for Ion Channel Recordings"],["dc.type","book_chapter"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1816"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Langmuir"],["dc.bibliographiccitation.lastpage","1823"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Reiss, Björn"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Seebach, Jochen"],["dc.contributor.author","Wegener, Joachim"],["dc.date.accessioned","2017-09-07T11:45:04Z"],["dc.date.available","2017-09-07T11:45:04Z"],["dc.date.issued","2003"],["dc.description.abstract","The suitability of the quartz crystal microbalance technique (QCM) to monitor the formation and modulation of cell- substrate contacts in real time has recently been established. A more detailed analysis of the QCM response when living cells attach and spread on the resonator surfaces is, however, hampered by the chemical and mechanical complexity of cellular systems and the experimental difficulties to control one single parameter of cell-substrate contacts in a predictable way. In this study, we made use of liposomes as simple cell models and studied the interactions of these liposomes with the resonator surface. To mimic the specific interactions between cell and protein-coated substrate as given in cell culture experiments, we incorporated biotin-labeled lipids as \"receptors\" in the liposome shell and preadsorbed avidin on the resonator surface. The dissipational QCM (D-QCM) technology was applied to monitor the shifts in resonance frequency and energy dissipation during the adsorption of liposomes prepared with increasing amounts of biotin-labeled lipids. We also studied the adsorption kinetics of liposomes doped with biotin moieties that were attached to the lipid core by an alkyl spacer in order to increase the distance between liposome shell and resonator surface. A comparison of these data with the adhesion kinetics of mammalian cells as monitored by D-QCM is presented and discussed. Although the shifts in resonance frequency are very similar for intact liposomes and mammalian cells, the viscous energy dissipation is significantly higher when cells attach and spread on the resonator surface."],["dc.identifier.doi","10.1021/la0261747"],["dc.identifier.gro","3144124"],["dc.identifier.isi","000181309600049"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1714"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0743-7463"],["dc.title","Adhesion kinetics of functionalized vesicles and mammalian cells: A comparative study"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2287"],["dc.bibliographiccitation.issue","13-14"],["dc.bibliographiccitation.journal","Journal of Adhesion Science and Technology"],["dc.bibliographiccitation.lastpage","2300"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Lorenz, Bärbel"],["dc.contributor.author","Pietuch, Anna"],["dc.contributor.author","Fine, Tamir"],["dc.contributor.author","Tarantola, Marco"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Wegener, Joachim"],["dc.date.accessioned","2017-09-07T11:46:42Z"],["dc.date.available","2017-09-07T11:46:42Z"],["dc.date.issued","2010"],["dc.description.abstract","The adhesion of MDCK II cells to porous and non-porous silicon substrates has been investigated by means of fluorescence and atomic force microscopy. The MDCK II cell density and the average height of the cells were increased on porous silicon substrates with regular 1.2 mu m pores as compared to flat, non-porous surfaces. In addition, we found a substantially reduced actin cytoskeleton within confluent cells cultured on the macroporous substrate compared to flat surfaces. The perturbation of the cytoskeleton relates to a significantly reduced expression of integrins on the porous area. The loss of stress fibers and cortical actin is accompanied by a dramatically reduced Young's modulus of 0.15 kPa compared to 6 kPa on flat surfaces as revealed by site-specific force-indentation experiments. (C) Koninklijke Brill NV, Leiden, 2010"],["dc.identifier.doi","10.1163/016942410X508028"],["dc.identifier.gro","3142996"],["dc.identifier.isi","000284152300013"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/462"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0169-4243"],["dc.title","Cell Adhesion to Ordered Pores: Consequences for Cellular Elasticity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","126a"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Schön, Markus"],["dc.contributor.author","Kramer, Corinna"],["dc.contributor.author","Noeding, Helen"],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2020-12-10T14:22:43Z"],["dc.date.available","2020-12-10T14:22:43Z"],["dc.date.issued","2016"],["dc.format.extent","126A"],["dc.identifier.doi","10.1016/j.bpj.2015.11.727"],["dc.identifier.isi","000375093800128"],["dc.identifier.issn","0006-3495"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71703"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.publisher.place","Cambridge"],["dc.relation.eventlocation","Los Angeles, CA"],["dc.relation.issn","1542-0086"],["dc.relation.issn","0006-3495"],["dc.title","Self-Organization of Actomyosin Networks Attached to Artificial Membranes"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1865"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Measurement Science and Technology"],["dc.bibliographiccitation.lastpage","1875"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Lüthgens, Eike"],["dc.contributor.author","Herrig, Alexander"],["dc.contributor.author","Kastl, Katja"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Reiss, Björn"],["dc.contributor.author","Wegener, Joachim"],["dc.contributor.author","Pignataro, Bruno"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2017-09-07T11:44:09Z"],["dc.date.available","2017-09-07T11:44:09Z"],["dc.date.issued","2003"],["dc.description.abstract","Three different systems are presented, exploring the adhesion of liposomes mediated by electrostatic and lipid-protein interactions as well as molecular recognition of ligand receptor pairs. Liposomes are frequently used to gain insight into the complicated processes involving adhesion and subsequent events such as fusion and fission mainly triggered by specific proteins. We combined liposome technology with the quartz crystal microbalance (QCM) technique as a powerful tool to study the hidden interface between the membrane and functionalized surface. Electrostatic attraction and molecular recognition were employed to bind liposomes to the functionalized quartz crystal. The QCM was used to distinguish between adsorption of vesicles and rupture due to strong adhesive forces. Intact vesicles display viscoelastic behaviour, while planar lipid bilayers as a result of vesicle rupture can be modelled by a thin rigid film. Furthermore, the adhesion of cells was modelled successfully by receptor bearing liposomes. Scanning force microscopy was used to confirm the results obtained by QCM measurements."],["dc.identifier.doi","10.1088/0957-0233/14/11/003"],["dc.identifier.gro","3144042"],["dc.identifier.isi","000187238900004"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1622"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1361-6501"],["dc.relation.issn","0957-0233"],["dc.title","Adhesion of liposomes: a quartz crystal microbalance study"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","213"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Bioelectrochemistry and Bioenergetics"],["dc.bibliographiccitation.lastpage","220"],["dc.bibliographiccitation.volume","42"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Galla, Hans-Joachim"],["dc.contributor.author","Sieber, Manfred"],["dc.date.accessioned","2017-09-07T11:50:58Z"],["dc.date.available","2017-09-07T11:50:58Z"],["dc.date.issued","1997"],["dc.description.abstract","The topic of this study is a solid supported lipid bilayer consisting of dimethyldioctadecylammoniumbromide (DODAB) and the channel-forming polypeptide, gramicidin D, from Bacillus brevis immobilized on gold electrodes. The peptide was reconstituted into large unilamellar vesicles of DODAB which were fused on a negatively charged monolayer of 3-mercaptopropionic acid. The peptide forms a pore of 4 Angstrom diameter, selective for monovalent cations. The sequence of conductivity of monovalent alkaline cations is Cs+ > K+ > Na+ > Li+. The transport of these monovalent cations through this supported lipid bilayer via the gramicidin dimer was observed by a.c. impedance spectroscopy as an integral electrochemical method. Only a single bilayer preparation was necessary to perform the whole measurement. The obtained data were analysed with an equivalent circuit based on the theory developed by de Levie. We succeeded in confirming the sequence of the conductivity by impedance spectroscopy. The conductance of the membrane shows a linear dependence on the concentration of the cations in the bulk phase. This system is therefore recommended for biosensor devices based on ion transport through solid supported membranes. (C) 1997 Elsevier Science S.A."],["dc.identifier.doi","10.1016/S0302-4598(96)05113-6"],["dc.identifier.gro","3144603"],["dc.identifier.isi","A1997XM00500016"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2246"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0302-4598"],["dc.title","Impedance analysis of ion transport through gramicidin channels incorporated in solid supported lipid bilayers"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","141"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Chemistry and Physics of Lipids"],["dc.bibliographiccitation.lastpage","152"],["dc.bibliographiccitation.volume","89"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Hohn, Fredrick"],["dc.contributor.author","Sieber, Manfred"],["dc.contributor.author","Galla, Hans-Joachim"],["dc.date.accessioned","2017-09-07T11:48:15Z"],["dc.date.available","2017-09-07T11:48:15Z"],["dc.date.issued","1997"],["dc.description.abstract","Bacteriorhodopsin (BR) was incorporated in solid supported lipid bilayers by fusion of reverse phase vesicles on chemisorbed monolayers of 1,2-dimyristoyl-sn-glycero-3-phosphothioethanol (DMPTE) on gold substrates. The passive electrical behavior of the artificial membranes was monitored by impedance spectroscopy in order to determine both the membrane resistances and capacitances and to guarantee reproducibility of the bilayer formation. Illumination of the BR containing solid supported lipid bilayers resulted in a transient photocurrent as expected from earlier experiments with black lipid membranes. The present preparation technique however is advantageous because of its long term stability up to 1 day without loss of BR activity and its easy handling. We investigated the dependence of the photocurrent on the BR content, lipid environment, pH, and a proton carrier using a common current amplifier. Maximum current densities were obtained in the presence of negatively charged lipids like 1,2-dimyristoyl-sn-glycero-3-phosphatidic acid (DMPA) or 1-palmitoyl-2-sn-glycero-3-phosphoglycerol (POPG) at a pH of 6.4. Moreover it could be shown that the pump activity of reconstituted BR is insignificantly influenced by the capacitance of the first self-assembled DMPTE-monolayer on the gold electrodes. This may be explained by an incomplete fusion of BR containing vesicles on the hydrophobic surface. Carbonylcyanid-4-trifluoromethoxy-phenylhydrazone (FCCP), a membrane soluble proton translocator, increases the membrane conductance as well as the capacitance of the lipid bilayer that was derived either from impedance spectroscopy or evaluation of the time constants of the transient photocurrents. (C) 1997 Elsevier Science Ireland Ltd."],["dc.identifier.doi","10.1016/S0009-3084(97)00071-6"],["dc.identifier.gro","3144586"],["dc.identifier.isi","A1997YE29200007"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2226"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0009-3084"],["dc.title","Proton translocation across bacteriorhodopsin containing solid supported lipid bilayers"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","6329"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Nano Letters"],["dc.bibliographiccitation.lastpage","6335"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Hubrich, Hanna"],["dc.contributor.author","Mey, Ingo P."],["dc.contributor.author","Brückner, Bastian R."],["dc.contributor.author","Mühlenbrock, Peter"],["dc.contributor.author","Nehls, Stefan"],["dc.contributor.author","Grabenhorst, Lennart"],["dc.contributor.author","Oswald, Tabea"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2020-11-05T15:08:07Z"],["dc.date.available","2020-11-05T15:08:07Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1021/acs.nanolett.0c01769"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/68468"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-352.7"],["dc.relation.eissn","1530-6992"],["dc.relation.issn","1530-6984"],["dc.title","Viscoelasticity of Native and Artificial Actin Cortices Assessed by Nanoindentation Experiments"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","11259"],["dc.bibliographiccitation.issue","49"],["dc.bibliographiccitation.journal","Tetrahedron"],["dc.bibliographiccitation.lastpage","11267"],["dc.bibliographiccitation.volume","60"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Lin, Victor S.-Y."],["dc.contributor.author","Völcker, Nicolas H."],["dc.contributor.author","Ghadiri, M. Reza"],["dc.date.accessioned","2017-09-07T11:43:10Z"],["dc.date.available","2017-09-07T11:43:10Z"],["dc.date.issued","2004"],["dc.description.abstract","Hybridization of DNA oligonucleotides in neutral aqueous solutions with complementary sequences immobilized on highly doped p-type porous silicon matrix is shown to result in an unexpectedly large shift in the Fabry-Perot interference pattern to lower wavelengths implying a decrease in effective optical thickness of the porous matrix. We have determined that the observed optical effects are due to enhanced corrosion (oxidation-hydrolysis) of the porous silicon layer triggered by the formation of complementary DNA duplexes. Scanning force microscopy and reflectance spectroscopy were employed at various stages of the signal evolution process to monitor and establish the material changes induced by the DNA binding events. We postulate that the slow background corrosion process initiated at the exposed Si-H-x, groups is dramatically enhanced as a result of the change in carrier charge density of the porous silicon layer in response to the local increase in the electrostatic field generated by the nucleic acid hybridization. The proposed mechanism is consistent with the experimental observations that the characteristics of the porous silicon matrix and the charge density of the hybridized DNA complexes can both influence the corrosion process. Functionalized porous silicon matrices prepared from highly doped silicon wafers (resistivity 1 mOmega(.)cm) produce large corrosion rates and improved signal to noise ratios. Moreover, the enhanced decrease in the effective optical thickness could be prevented by either shielding the negative charges of the DNA duplex in the presence of Mg2+ ions, or by using backbone charge neutral peptide nucleic acids (PNA) in the DNA hybridization experiments. The observed phenomenon is thus an example of an active sensor matrix in which the molecular recognition signal is transduced and amplified by a profound change in the chemical reactivity and physical property of the solid support itself. With the signal amplification mechanism described, binding of unlabeled complementary DNA oligonucleotides of approximately 0.1 amol/mm(2) has been detected suggesting the potential utility of this new approach in DNA sensing. (C) 2004 Elsevier Ltd. All rights reserved."],["dc.identifier.doi","10.1016/j.tet.2004.06.130"],["dc.identifier.gro","3143928"],["dc.identifier.isi","000225053700024"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1496"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0040-4020"],["dc.title","DNA hybridization-enhanced porous silicon corrosion: mechanistic investigators and prospect for optical interferometric biosensing"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5624"],["dc.bibliographiccitation.issue","14"],["dc.bibliographiccitation.journal","Analytical Chemistry"],["dc.bibliographiccitation.lastpage","5630"],["dc.bibliographiccitation.volume","83"],["dc.contributor.author","Lazzara, Thomas D."],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2017-09-07T11:44:07Z"],["dc.date.available","2017-09-07T11:44:07Z"],["dc.date.issued","2011"],["dc.description.abstract","Porous substrates have gained widespread interest for biosensor applications based on molecular recognition. Thus, there is a great demand to systematically investigate the parameters that limit the transport of molecules toward and within the porous matrix as a function of pore geometry. Finite element simulations (FES) and time-resolved optical waveguide spectroscopy (OWS) experiments were used to systematically study the transport of molecules and their binding on ism the inner surface of a porous material. OWS allowed us to measure the kinetics of protein adsorption within porous anodic aluminum oxide membranes composed of parallel-aligned, cylindrical pores with pore radii of 10-40 nm and pore depths of 0.8-9.6 mu m. FES showed that protein adsorption on the inner surface of a porous matrix is almost exclusively governed by the flux into the pores. The pore-interior surface nearly acts as a perfect sink for the macromolecules. Neither diffusion within the pores nor adsorption on the surface are rate limiting steps, except for very low rate constants of adsorption. While adsorption on the pore walls is mainly governed by the stationary flux into the pores, desorption from the inner pore walls involves the rate constants of desorption and adsorption, essentially representing the protein surface interaction potential. FES captured the essential features of the OWS experiments such as the initial linear slopes of the adsorption kinetics, which are inversely proportional to the pore depth and linearly proportional to protein concentration. We show that protein adsorption kinetics allows for an accurate determination of protein concentration, while desorption kinetics could be used to capture the interaction potential of the macromolecules with the pore walls."],["dc.identifier.doi","10.1021/ac200725y"],["dc.identifier.gro","3142695"],["dc.identifier.isi","000292892000021"],["dc.identifier.pmid","21651041"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9415"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/128"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0003-2700"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Benefits and Limitations of Porous Substrates as Biosensors for Protein Adsorption"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]