Kruss, Sebastian

[["dc.bibliographiccitation.firstpage","528"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Molecular Cancer Research"],["dc.bibliographiccitation.lastpage","542"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Amschler, Katharina"],["dc.contributor.author","Kossmann, Eugen"],["dc.contributor.author","Erpenbeck, Luise"],["dc.contributor.author","Kruss, Sebastian"],["dc.contributor.author","Schill, Tillmann"],["dc.contributor.author","Schön, Margarete"],["dc.contributor.author","Möckel, Sigrid M.C."],["dc.contributor.author","Spatz, Joachim P."],["dc.contributor.author","Schön, Michael P."],["dc.date.accessioned","2020-12-10T18:37:47Z"],["dc.date.available","2020-12-10T18:37:47Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1158/1541-7786.MCR-17-0272"],["dc.identifier.eissn","1557-3125"],["dc.identifier.issn","1541-7786"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77091"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Nanoscale Tuning of VCAM-1 Determines VLA-4–Dependent Melanoma Cell Plasticity on RGD Motifs"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Experimental Dermatology"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Erpenbeck, Luise"],["dc.contributor.author","Kruss, Sebastian"],["dc.contributor.author","Amschler, Katharina"],["dc.contributor.author","Spear, Stephen F."],["dc.contributor.author","Schoen, Michael Peter"],["dc.date.accessioned","2018-11-07T09:43:01Z"],["dc.date.available","2018-11-07T09:43:01Z"],["dc.date.issued","2014"],["dc.format.extent","E11"],["dc.identifier.isi","000332335500079"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34086"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.conference","41st Annual Meeting of the Arbeitsgemeinschaft-Dermatologische-Forschung (ADF)"],["dc.relation.eventlocation","Cologne, GERMANY"],["dc.relation.issn","1600-0625"],["dc.relation.issn","0906-6705"],["dc.title","Adhesion maturation of neutrophils on nanoscopically presented integrin ligands"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Experimental Dermatology"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Amschler, Katharina"],["dc.contributor.author","Kossmann, E."],["dc.contributor.author","Erpenbeck, Luise"],["dc.contributor.author","Spear, Stephen F."],["dc.contributor.author","Kruss, Sebastian"],["dc.contributor.author","Schoen, Michael Peter"],["dc.date.accessioned","2018-11-07T09:43:00Z"],["dc.date.available","2018-11-07T09:43:00Z"],["dc.date.issued","2014"],["dc.format.extent","E46"],["dc.identifier.isi","000332335500287"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34084"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.conference","41st Annual Meeting of the Arbeitsgemeinschaft-Dermatologische-Forschung (ADF)"],["dc.relation.eventlocation","Cologne, GERMANY"],["dc.relation.issn","1600-0625"],["dc.relation.issn","0906-6705"],["dc.title","Melanoma cell function regulated by VCAM-1 presented on tunable nano-structured surfaces"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","17693"],["dc.bibliographiccitation.issue","21"],["dc.bibliographiccitation.journal","ACS Applied Materials & Interfaces"],["dc.bibliographiccitation.lastpage","17703"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Polo, Elena"],["dc.contributor.author","Nitka, Tadeusz T."],["dc.contributor.author","Neubert, Elsa"],["dc.contributor.author","Erpenbeck, Luise"],["dc.contributor.author","Vuković, Lela"],["dc.contributor.author","Kruss, Sebastian"],["dc.date.accessioned","2020-12-10T15:22:29Z"],["dc.date.available","2020-12-10T15:22:29Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1021/acsami.8b04373"],["dc.identifier.eissn","1944-8252"],["dc.identifier.issn","1944-8244"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73418"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Control of Integrin Affinity by Confining RGD Peptides on Fluorescent Carbon Nanotubes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","147"],["dc.bibliographiccitation.journal","Carbon"],["dc.bibliographiccitation.lastpage","153"],["dc.bibliographiccitation.volume","97"],["dc.contributor.author","Salem, Daniel P."],["dc.contributor.author","Landry, Markita P."],["dc.contributor.author","Bisker, Gili"],["dc.contributor.author","Ahn, Jiyoung"],["dc.contributor.author","Kruss, Sebastian"],["dc.contributor.author","Strano, Michael S."],["dc.date.accessioned","2018-11-07T10:19:04Z"],["dc.date.available","2018-11-07T10:19:04Z"],["dc.date.issued","2016"],["dc.description.abstract","Corona phase molecular recognition (CoPhMoRe) is a phenomenon whereby a polymer or surfactant corona phase wrapped around a nanoparticle selectively recognizes a particular molecule. The method can potentially generate non-biological, synthetic molecular recognition sites, analogous to antibodies, for a broad range of biomedical applications, including new types of sensors, laboratory and clinical assays, as well as inhibitors and targeted therapeutics. In this work, we utilize near infrared fluorescent single-walled carbon nanotubes (SWNTs) wrapped with specific single stranded DNA sequences to explore the (n,m) chirality dependence of CoPhMoRe. Specific DNA oligonucleotide sequences are known to recognize and interact uniquely with certain (n, m) SWNTs enabling their enrichment in ion exchange chromatography. We explore the CoPhMoRe effect using corona phases constructed from a library of 24 such sequences, screening against a biomolecule panel that includes common neurotransmitters, amino acids, saccharides and riboflavin. Example sequences include (ATT)(4), (TAT)(4) and (ATTT)(3) which recognize (7,5), (6,5) and (8,4) SWNTs, respectively. We find that these recognition sequences indeed form CoPhMoRe phases that are distinct among SWNT chiralities, and appear to pack more densely as to exclude analyte adsorption on the chirality they recognize. These results have encouraging implications for the controlled design of CoPhMoRe phases for biomedical applications. (C) 2015 Elsevier Ltd. All rights reserved."],["dc.identifier.doi","10.1016/j.carbon.2015.08.075"],["dc.identifier.isi","000366939900016"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41587"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Pergamon-elsevier Science Ltd"],["dc.relation.issn","1873-3891"],["dc.relation.issn","0008-6223"],["dc.title","Chirality dependent corona phase molecular recognition of DNA-wrapped carbon nanotubes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","9984"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","ACS Nano"],["dc.bibliographiccitation.lastpage","9996"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Kruss, Sebastian"],["dc.contributor.author","Erpenbeck, Luise"],["dc.contributor.author","Amschler, Katharina"],["dc.contributor.author","Mundinger, Tabea A."],["dc.contributor.author","Boehm, Heike"],["dc.contributor.author","Helms, Hans-Joachim"],["dc.contributor.author","Friede, Tim"],["dc.contributor.author","Andrews, Robert K."],["dc.contributor.author","Schoen, Michael Peter"],["dc.contributor.author","Spatz, Joachim P."],["dc.date.accessioned","2021-08-17T14:20:35Z"],["dc.date.available","2021-08-17T14:20:35Z"],["dc.date.issued","2013"],["dc.description.abstract","Neutrophilic granulocytes play a fundamental role in cardiovascular disease. They interact with platelet aggregates via the integrin Mac-1 and the platelet receptor glycoprotein Ibα (GPIbα). In vivo, GPIbα presentation is highly variable under different physiological and pathophysiological conditions. Here, we quantitatively determined the conditions for neutrophil adhesion in a biomimetic in vitro system, which allowed precise adjustment of the spacings between human GPIbα presented on the nanoscale from 60 to 200 nm. Unlike most conventional nanopatterning approaches, this method provided control over the local receptor density (spacing) rather than just the global receptor density. Under physiological flow conditions, neutrophils required a minimum spacing of GPIbα molecules to successfully adhere. In contrast, under low-flow conditions, neutrophils adhered on all tested spacings with subtle but nonlinear differences in cell response, including spreading area, spreading kinetics, adhesion maturation, and mobility. Surprisingly, Mac-1-dependent neutrophil adhesion was very robust to GPIbα density variations up to 1 order of magnitude. This complex response map indicates that neutrophil adhesion under flow and adhesion maturation are differentially regulated by GPIbα density. Our study reveals how Mac-1/GPIbα interactions govern cell adhesion and how neutrophils process the number of available surface receptors on the nanoscale. In the future, such in vitro studies can be useful to determine optimum therapeutic ranges for targeting this interaction."],["dc.identifier.doi","10.1021/nn403923h"],["dc.identifier.isi","000327752200047"],["dc.identifier.pmid","24093566"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/88782"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Chemical Soc"],["dc.relation.eissn","1936-086X"],["dc.relation.issn","1936-0851"],["dc.relation.issn","1936-086X"],["dc.title","Adhesion maturation of neutrophils on nanoscopically presented platelet glycoprotein Ibα"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Molecular Neurobiology"],["dc.contributor.author","Noor, Aneeqa"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Shafiq, Mohsin"],["dc.contributor.author","Younas, Neelam"],["dc.contributor.author","Siegert, Anna"],["dc.contributor.author","Mann, Florian A."],["dc.contributor.author","Kruss, Sebastian"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Ferrer, Isidre"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2021-12-01T09:23:29Z"],["dc.date.available","2021-12-01T09:23:29Z"],["dc.date.issued","2021"],["dc.description.abstract","Abstract The molecular determinants of atypical clinical variants of Alzheimer’s disease, including the recently discovered rapidly progressive Alzheimer’s disease (rpAD), are unknown to date. Fibrilization of the amyloid-β (Aβ) peptide is the most frequently studied candidate in this context. The Aβ peptide can exist as multiple proteoforms that vary in their post-translational processing, amyloidogenesis, and toxicity. The current study was designed to identify these variations in Alzheimer’s disease patients exhibiting classical (sAD) and rapid progression, with the primary aim of establishing if these variants may constitute strains that underlie the phenotypic variability of Alzheimer’s disease. We employed two-dimensional polyacrylamide gel electrophoresis and MALDI-ToF mass spectrometry to validate and identify the Aβ proteoforms extracted from targeted brain tissues. The biophysical analysis was conducted using RT-QuIC assay, confocal microscopy, and atomic force microscopy. Interactome analysis was performed by co-immunoprecipitation. We present a signature of 33 distinct pathophysiological proteoforms, including the commonly targeted Aβ 40 , Aβ 42 , Aβ 4-42 , Aβ 11-42 , and provide insight into their synthesis and quantities. Furthermore, we have validated the presence of highly hydrophobic Aβ seeds in rpAD brains that seeded reactions at a slower pace in comparison to typical Alzheimer’s disease. In vitro and in vivo analyses also verified variations in the molecular pathways modulated by brain-derived Aβ. These variations in the presence, synthesis, folding, and interactions of Aβ among sAD and rpAD brains constitute important points of intervention. Further validation of reported targets and mechanisms will aid in the diagnosis of and therapy for Alzheimer’s disease."],["dc.description.abstract","Abstract The molecular determinants of atypical clinical variants of Alzheimer’s disease, including the recently discovered rapidly progressive Alzheimer’s disease (rpAD), are unknown to date. Fibrilization of the amyloid-β (Aβ) peptide is the most frequently studied candidate in this context. The Aβ peptide can exist as multiple proteoforms that vary in their post-translational processing, amyloidogenesis, and toxicity. The current study was designed to identify these variations in Alzheimer’s disease patients exhibiting classical (sAD) and rapid progression, with the primary aim of establishing if these variants may constitute strains that underlie the phenotypic variability of Alzheimer’s disease. We employed two-dimensional polyacrylamide gel electrophoresis and MALDI-ToF mass spectrometry to validate and identify the Aβ proteoforms extracted from targeted brain tissues. The biophysical analysis was conducted using RT-QuIC assay, confocal microscopy, and atomic force microscopy. Interactome analysis was performed by co-immunoprecipitation. We present a signature of 33 distinct pathophysiological proteoforms, including the commonly targeted Aβ 40 , Aβ 42 , Aβ 4-42 , Aβ 11-42 , and provide insight into their synthesis and quantities. Furthermore, we have validated the presence of highly hydrophobic Aβ seeds in rpAD brains that seeded reactions at a slower pace in comparison to typical Alzheimer’s disease. In vitro and in vivo analyses also verified variations in the molecular pathways modulated by brain-derived Aβ. These variations in the presence, synthesis, folding, and interactions of Aβ among sAD and rpAD brains constitute important points of intervention. Further validation of reported targets and mechanisms will aid in the diagnosis of and therapy for Alzheimer’s disease."],["dc.identifier.doi","10.1007/s12035-021-02566-9"],["dc.identifier.pii","2566"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94665"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.relation.eissn","1559-1182"],["dc.relation.issn","0893-7648"],["dc.title","Molecular Profiles of Amyloid-β Proteoforms in Typical and Rapidly Progressive Alzheimer’s Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","E15"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Experimental Dermatology"],["dc.bibliographiccitation.lastpage","E16"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Kwaczala-Tessmann, A."],["dc.contributor.author","Senger-Sander, S. N."],["dc.contributor.author","Neubert, E."],["dc.contributor.author","Meyer, D."],["dc.contributor.author","Schoen, Michael Peter"],["dc.contributor.author","Kruss, Sebastian"],["dc.contributor.author","Erpenbeck, Luise"],["dc.date.accessioned","2018-11-07T10:26:25Z"],["dc.date.available","2018-11-07T10:26:25Z"],["dc.date.issued","2017"],["dc.identifier.isi","000397284200037"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43038"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley"],["dc.publisher.place","Hoboken"],["dc.relation.conference","44th Annual Meeting of the Arbeitsgemeinschaft-Dermatologische-Forschung (ADF)"],["dc.relation.eventlocation","Gottingen, GERMANY"],["dc.relation.issn","1600-0625"],["dc.relation.issn","0906-6705"],["dc.title","Cytoskeletal reorganization during NET formation"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3061"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","The Journal of Physical Chemistry C"],["dc.bibliographiccitation.lastpage","3070"],["dc.bibliographiccitation.volume","120"],["dc.contributor.author","Polo, Elena"],["dc.contributor.author","Kruss, Sebastian"],["dc.date.accessioned","2018-11-07T10:18:15Z"],["dc.date.available","2018-11-07T10:18:15Z"],["dc.date.issued","2016"],["dc.description.abstract","The near-infrared (nIR) fluorescence of polymer-wrapped single-walled carbon nanotubes (SWCNTs) is very sensitive to the local chemical environment. It has been shown that certain small reducing molecules can increase the fluorescence of SWCNTs. However, so far the role of the polymer around the SWCNT as well as the mechanism is not understood. Here, we investigated how reducing and oxidizing small molecules affect the nIR fluorescence of polymer-wrapped SWCNTs. Our results show that the polymer plays an essential role. Reducing molecules such as ascorbic acid, epinephrine, and trolox increased the nIR fluorescence up to 250% but only if SWCNTs were suspended in negatively charged polymers such as DNA or poly(acrylic acid) (PAA). In comparison, phospholipid poly(ethylene glycol) wrapped SWCNTs did not respond at all while positively charged polyallylamine-wrapped SWCNTs were quenched. Oxidized equivalents such as dehydroascorbic acid did not show a clear tendency to quench or increase fluorescence. Only riboflavin with an intermediate oxidation potential and light absorption in the visible range quenched all polymer wrapped SWCNTs. In general, polymer-wrapped SWCNTs that responded to reducing molecules (e.g., +141%, ascorbic acid) also responded to oxidizing molecules (e.g., -81%, riboflavin). Nevertheless, several reducing molecules showed only a small fluorescence increase (NADH, +21%) or even a decrease (glutathione, -14%), which highlights that the redox potential alone cannot explain fluorescence changes. Furthermore, we show that neither changes of absorption cross sections, scavenging of reactive oxygen species (ROS), nor free surface areas on SWCNTs explain the observed patterns. However, results are in agreement either with a redox reaction of the polymer or conformational changes of the polymer that change fluorescence decay routes. In summary, we show that the polymer around SWCNTs governs how redox-active molecules change nIR fluorescence (quantum yield) of SWCNTs. Molecules with a low redox potential (<-0.4 V) are more likely to increase SWCNT fluorescence, but a low redox-potential alone is not sufficient."],["dc.description.sponsorship","Liebig fellowship (Fonds der chemischen Industrie)"],["dc.identifier.doi","10.1021/acs.jpcc.5b12183"],["dc.identifier.isi","000370210400065"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41399"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","1932-7447"],["dc.title","Impact of Redox-Active Molecules on the Fluorescence of Polymer-Wrapped Carbon Nanotubes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2727"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Analytical and Bioanalytical Chemistry"],["dc.bibliographiccitation.lastpage","2741"],["dc.bibliographiccitation.volume","408"],["dc.contributor.author","Polo, Elena"],["dc.contributor.author","Kruss, Sebastian"],["dc.date.accessioned","2018-11-07T10:16:13Z"],["dc.date.available","2018-11-07T10:16:13Z"],["dc.date.issued","2016"],["dc.description.abstract","Neurotransmitters are an important class of messenger molecules. They govern chemical communication between cells for example in the brain. The spatiotemporal propagation of these chemical signals is a crucial part of communication between cells. Thus, the spatial aspect of neurotransmitter release is equally important as the mere time-resolved measurement of these substances. In conclusion, without tools that provide the necessary spatiotemporal resolution, chemical signaling via neurotransmitters cannot be studied in greater detail. In this review article we provide a critical overview about sensors/probes that are able to monitor neurotransmitters. Our focus are sensing concepts that provide or could in the future provide the spatiotemporal resolution that is necessary to 'image' dynamic changes of neurotransmitter concentrations around cells. These requirements set the bar for the type of sensors we discuss. The sensor must be small enough (if possible on the nanoscale) to provide the envisioned spatial resolution and it should allow parallel (spatial) detection. In this article we discuss both optical and electrochemical concepts that meet these criteria. We cover techniques that are based on fluorescent building blocks such as nanomaterials, proteins and organic dyes. Additionally, we review electrochemical array techniques and assess limitations and possible future directions."],["dc.description.sponsorship","Fonds der chemischen Industrie (FCI)"],["dc.identifier.doi","10.1007/s00216-015-9160-x"],["dc.identifier.isi","000374110700010"],["dc.identifier.pmid","26586160"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40996"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","Heidelberg"],["dc.relation.issn","1618-2650"],["dc.relation.issn","1618-2642"],["dc.title","Nanosensors for neurotransmitters"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]