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Kruss, Sebastian
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Kruss, Sebastian
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Kruss, Sebastian
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Kruss, S.
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2016Journal Article [["dc.bibliographiccitation.artnumber","10241"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Bisker, Gili"],["dc.contributor.author","Dong, Juyao"],["dc.contributor.author","Park, Hoyoung D."],["dc.contributor.author","Iverson, Nicole M."],["dc.contributor.author","Ahn, Jiyoung"],["dc.contributor.author","Nelson, Justin T."],["dc.contributor.author","Landry, Markita P."],["dc.contributor.author","Kruss, Sebastian"],["dc.contributor.author","Strano, Michael S."],["dc.date.accessioned","2018-11-07T10:21:13Z"],["dc.date.available","2018-11-07T10:21:13Z"],["dc.date.issued","2016"],["dc.description.abstract","Corona phase molecular recognition (CoPhMoRe) uses a heteropolymer adsorbed onto and templated by a nanoparticle surface to recognize a specific target analyte. This method has not yet been extended to macromolecular analytes, including proteins. Herein we develop a variant of a CoPhMoRe screening procedure of single-walled carbon nanotubes (SWCNT) and use it against a panel of human blood proteins, revealing a specific corona phase that recognizes fibrinogen with high selectivity. In response to fibrinogen binding, SWCNT fluorescence decreases by 480% at saturation. Sequential binding of the three fibrinogen nodules is suggested by selective fluorescence quenching by isolated sub-domains and validated by the quenching kinetics. The fibrinogen recognition also occurs in serum environment, at the clinically relevant fibrinogen concentrations in the human blood. These results open new avenues for synthetic, non-biological antibody analogues that recognize biological macromolecules, and hold great promise for medical and clinical applications."],["dc.identifier.doi","10.1038/ncomms10241"],["dc.identifier.isi","000369018800004"],["dc.identifier.pmid","26742890"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12894"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42048"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","2041-1723"],["dc.relation.orgunit","Fakultät für Physik"],["dc.rights","CC BY 4.0"],["dc.title","Protein-targeted corona phase molecular recognition"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2020Journal Article Research Paper [["dc.bibliographiccitation.firstpage","9104-9115"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","Nanoscale"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Meyer, Daniel"],["dc.contributor.author","Telele, Saba"],["dc.contributor.author","Zelená, Anna"],["dc.contributor.author","Gillen, Alice J."],["dc.contributor.author","Antonucci, Alessandra"],["dc.contributor.author","Neubert, Elsa"],["dc.contributor.author","Nißler, Robert"],["dc.contributor.author","Mann, Florian A."],["dc.contributor.author","Erpenbeck, Luise"],["dc.contributor.author","Boghossian, Ardemis A."],["dc.contributor.author","Köster, Sarah"],["dc.contributor.author","Kruss, Sebastian"],["dc.date.accessioned","2020-06-26T11:13:39Z"],["dc.date.available","2020-06-26T11:13:39Z"],["dc.date.issued","2020"],["dc.description.abstract","Cells can take up nanoscale materials, which has important implications for understanding cellular functions, biocompatibility as well as biomedical applications. Controlled uptake, transport and triggered release of nanoscale cargo is one of the great challenges in biomedical applications of nanomaterials. Here, we study how human immune cells (neutrophilic granulocytes, neutrophils) take up nanomaterials and program them to release this cargo after a certain time period. For this purpose, we let neutrophils phagocytose DNA-functionalized single-walled carbon nanotubes (SWCNTs) in vitro that fluoresce in the near infrared (980 nm) and serve as sensors for small molecules. Cells still migrate, follow chemical gradients and respond to inflammatory signals after uptake of the cargo. To program release, we make use of neutrophil extracellular trap formation (NETosis), a novel cell death mechanism that leads to chromatin swelling, subsequent rupture of the cellular membrane and release of the cell's whole content. By using the process of NETosis, we can program the time point of cargo release via the initial concentration of stimuli such as phorbol 12-myristate-13-acetate (PMA) or lipopolysaccharide (LPS). At intermediate stimulation, cells continue to migrate, follow gradients and surface cues for around 30 minutes and up to several hundred micrometers until they stop and release the SWCNTs. The transported and released SWCNT sensors are still functional as shown by subsequent detection of the neurotransmitter dopamine and reactive oxygen species (H2O2). In summary, we hijack a biological process (NETosis) and demonstrate how neutrophils transport and release functional nanomaterials."],["dc.identifier.doi","10.1039/d0nr00864h"],["dc.identifier.pmid","32286598"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/66755"],["dc.language.iso","en"],["dc.relation.eissn","2040-3372"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.rights","CC BY 3.0"],["dc.subject.gro","cellular biophysics"],["dc.title","Transport and programmed release of nanoscale cargo from cells by using NETosis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]Details DOI PMID PMC2018Journal Article [["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"]]Details DOI2014Conference Abstract [["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"]]Details WOS2014Conference Abstract [["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"]]Details WOS2018Journal Article [["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"]]Details DOI2019Journal Article [["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Biophotonics"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Spreinat, Alexander"],["dc.contributor.author","Selvaggio, Gabriele"],["dc.contributor.author","Erpenbeck, Luise"],["dc.contributor.author","Kruss, Sebastian"],["dc.date.accessioned","2019-12-05T14:29:38Z"],["dc.date.accessioned","2021-10-27T13:12:48Z"],["dc.date.available","2019-12-05T14:29:38Z"],["dc.date.available","2021-10-27T13:12:48Z"],["dc.date.issued","2019"],["dc.description.abstract","Multispectral imaging combines the spectral resolution of spectroscopy with the spatial resolution of imaging and is therefore very useful for biomedical applications. Currently, histological diagnostics use mainly stainings with standard dyes (eg, hematoxylin + eosin) to identify tumors. This method is not applicable in vivo and provides low amounts of chemical information. Biomolecules absorb near infrared light (NIR, 800-1700 nm) at different wavelengths, which could be used to fingerprint tissue. Here, we built a NIR multispectral absorption imaging setup to study skin tissue samples. NIR light (900-1500 nm) was used for homogenous wide-field transmission illumination and detected by a cooled InGaAs camera. In this setup, images I(x, y, λ) from dermatological samples (melanoma, nodular basal-cell carcinoma, squamous-cell carcinoma) were acquired to distinguish healthy from diseased tissue regions. In summary, we show the potential of multispectral NIR imaging for cancer diagnostics."],["dc.description.sponsorship","life@nano"],["dc.identifier.doi","10.1002/jbio.201960080"],["dc.identifier.eissn","1864-0648"],["dc.identifier.isbn","31602799"],["dc.identifier.issn","1864-063X"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16850"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/91723"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","WILEY‐VCH Verlag GmbH \\u0026 Co. KGaA"],["dc.relation.eissn","1864-0648"],["dc.relation.issn","1864-0648"],["dc.relation.issn","1864-063X"],["dc.relation.orgunit","Fakultät für Chemie"],["dc.rights","CC BY 4.0"],["dc.rights.access","openAccess"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject","diagnostics; histology; multispectral imaging; near infrared spectroscopy; skin cancer"],["dc.subject.ddc","540"],["dc.title","Multispectral near infrared absorption imaging for histology of skin cancer"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]Details DOI2016Journal Article [["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"]]Details DOI WOS2019Journal Article [["dc.bibliographiccitation.artnumber","12"],["dc.bibliographiccitation.journal","Frontiers in Immunology"],["dc.bibliographiccitation.volume","10"],["dc.contributor.affiliation","Neubert, Elsa; 1Department of Dermatology, Venereology and Allergology, University Medical Center Göttingen, Göttingen, Germany"],["dc.contributor.affiliation","Senger-Sander, Susanne N.; 1Department of Dermatology, Venereology and Allergology, University Medical Center Göttingen, Göttingen, Germany"],["dc.contributor.affiliation","Manzke, Veit S.; 1Department of Dermatology, Venereology and Allergology, University Medical Center Göttingen, Göttingen, Germany"],["dc.contributor.affiliation","Busse, Julia; 1Department of Dermatology, Venereology and Allergology, University Medical Center Göttingen, Göttingen, Germany"],["dc.contributor.affiliation","Polo, Elena; 2Institute of Physical Chemistry, University of Göttingen, Göttingen, Germany"],["dc.contributor.affiliation","Scheidmann, Sophie E. F.; 1Department of Dermatology, Venereology and Allergology, University Medical Center Göttingen, Göttingen, Germany"],["dc.contributor.affiliation","Schön, Michael P.; 1Department of Dermatology, Venereology and Allergology, University Medical Center Göttingen, Göttingen, Germany"],["dc.contributor.affiliation","Kruss, Sebastian; 2Institute of Physical Chemistry, University of Göttingen, Göttingen, Germany"],["dc.contributor.affiliation","Erpenbeck, Luise; 1Department of Dermatology, Venereology and Allergology, University Medical Center Göttingen, Göttingen, Germany"],["dc.contributor.author","Neubert, Elsa"],["dc.contributor.author","Senger-Sander, Susanne N."],["dc.contributor.author","Manzke, Veit S."],["dc.contributor.author","Busse, Julia"],["dc.contributor.author","Polo, Elena"],["dc.contributor.author","Scheidmann, Sophie E. F."],["dc.contributor.author","Schön, Michael P."],["dc.contributor.author","Kruss, Sebastian"],["dc.contributor.author","Erpenbeck, Luise"],["dc.date.accessioned","2019-07-09T11:50:03Z"],["dc.date.available","2019-07-09T11:50:03Z"],["dc.date.issued","2019"],["dc.date.updated","2022-02-09T13:23:16Z"],["dc.description.abstract","The formation of neutrophil extracellular traps (NETs) is an immune defense mechanism of neutrophilic granulocytes. Moreover, it is also involved in the pathogenesis of autoimmune, inflammatory, and neoplastic diseases. For that reason, the process of NET formation (NETosis) is subject of intense ongoing research. In vitro approaches to quantify NET formation are commonly used and involve neutrophil stimulation with various activators such as phorbol 12-myristate 13-acetate (PMA), lipopolysaccharides (LPS), or calcium ionophores (CaI). However, the experimental conditions of these experiments, particularly the media and media supplements employed by different research groups, vary considerably, rendering comparisons of results difficult. Here, we present the first standardized investigation of the influence of different media supplements on NET formation in vitro. The addition of heat-inactivated (hi) fetal calf serum (FCS), 0.5% human serum albumin (HSA), or 0.5% bovine serum albumin (BSA) efficiently prevented NET formation of human neutrophils following stimulation with LPS and CaI, but not after stimulation with PMA. Thus, serum components such as HSA, BSA and hiFCS (at concentrations typically found in the literature) inhibit NET formation to different degrees, depending on the NETosis inducer used. In contrast, in murine neutrophils, NETosis was inhibited by FCS and BSA, regardless of the inducer employed. This shows that mouse and human neutrophils have different susceptibilities toward the inhibition of NETosis by albumin or serum components. Furthermore, we provide experimental evidence that albumin inhibits NETosis by scavenging activators such as LPS. We also put our results into the context of media supplements most commonly used in NET research. In experiments with human neutrophils, either FCS (0.5-10%), heat-inactivated (hiFCS, 0.1-10%) or human serum albumin (HSA, 0.05-2%) was commonly added to the medium. For murine neutrophils, serum-free medium was used in most cases for stimulation with LPS and CaI, reflecting the different sensitivities of human and murine neutrophils to media supplements. Thus, the choice of media supplements greatly determines the outcome of experiments on NET-formation, which must be taken into account in NETosis research."],["dc.identifier.doi","10.3389/fimmu.2019.00012"],["dc.identifier.eissn","1664-3224"],["dc.identifier.pmid","30733715"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15847"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59691"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","Frontiers Media S.A."],["dc.relation.eissn","1664-3224"],["dc.relation.issn","1664-3224"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","Serum and Serum Albumin Inhibit in vitro Formation of Neutrophil Extracellular Traps (NETs)"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]Details DOI PMID PMC2013Journal Article Research Paper [["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"]]Details DOI PMID PMC WOS