SOLR
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1797818030227456000 |
| author |
Hennig, Stefan |
| author2 |
Rödel, Gerhard, Ostermann, Kai |
| author2_role |
, |
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g r gr, k o ko |
| author_facet |
Hennig, Stefan, Rödel, Gerhard, Ostermann, Kai |
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|
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Hennig, Stefan |
| author_variant |
s h sh |
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Library A |
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sid-22-col-qucosa |
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Sensors (2016), 16(5), ISSN 1424-8220. DOI: 10.3390/s16050602. Artikelnr.: 602 |
| contents |
Detection and quantification of small peptides, such as yeast pheromones, are often challenging. We developed a highly sensitive and robust affinity-assay for the quantification of the α-factor pheromone of Saccharomyces cerevisiae based on recombinant hydrophobins. These small, amphipathic proteins self-assemble into highly stable monolayers at hydrophilic-hydrophobic interfaces. Upon functionalization of solid supports with a combination of hydrophobins either lacking or exposing the α-factor, pheromone-specific antibodies were bound to the surface. Increasing concentrations of the pheromone competitively detached the antibodies, thus allowing for quantification of the pheromone. By adjusting the percentage of pheromone-exposing hydrophobins, the sensitivity of the assay could be precisely predefined. The assay proved to be highly robust against changes in sample matrix composition. Due to the high stability of hydrophobin layers, the functionalized surfaces could be repeatedly used without affecting the sensitivity. Furthermore, by using an inverse setup, the sensitivity was increased by three orders of magnitude, yielding a novel kind of biosensor for the yeast pheromone with the lowest limit of detection reported so far. This assay was applied to study the pheromone secretion of diverse yeast strains including a whole-cell biosensor strain of Schizosaccharomyces pombe modulating α-factor secretion in response to an environmental signal. |
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620 |
| dewey-hundreds |
600 - Technology (Applied sciences) |
| dewey-ones |
620 - Engineering and allied operations |
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620 |
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620 |
| dewey-sort |
3620 |
| dewey-tens |
620 - Engineering and allied operations |
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Online, Free |
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Technik |
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engineering-process, technology |
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ElectronicSerialComponentPart |
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Article, E-Article |
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Ebook |
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Article, E-Article |
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Article, E-Article |
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Buch |
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text-online-journal-child |
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Journal |
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Article, E-Article |
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ElectronicArticle |
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Article, E-Article |
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Article, E-Article |
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E-Article |
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not assigned |
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not assigned |
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Sensors (2016), 16(5), ISSN 1424-8220. DOI: 10.3390/s16050602. Artikelnr.: 602 |
| id |
22-14-qucosa-214807 |
| illustrated |
Not Illustrated |
| imprint |
Basel, Multidisciplinary Digital Publishing Institute (MDPI), 2016 |
| imprint_str_mv |
Online-Ausg.: 2017 |
| institution |
DE-105, DE-Gla1, DE-Brt1, DE-D161, DE-540, DE-Pl11, DE-Rs1, DE-Bn3, DE-Zi4, DE-Zwi2, DE-D117, DE-Mh31, DE-D275, DE-Ch1, DE-15, DE-D13, DE-L242, DE-L229, DE-L328 |
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English |
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2024-05-01T03:07:58.152Z |
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hennig2016hydrophobinbasedsurfaceengineeringforsensitiveandrobustquantificationofyeastpheromones |
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Qucosa |
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2016 |
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2016 |
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Basel |
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Multidisciplinary Digital Publishing Institute (MDPI) |
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14-qucosa-214807 |
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22 |
| spelling |
Hennig, Stefan, Hydrophobin-Based Surface Engineering for Sensitive and Robust Quantification of Yeast Pheromones, Basel Multidisciplinary Digital Publishing Institute (MDPI) 2016, Online-Ausg. 2017 Online-Ressource (Text) Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, Detection and quantification of small peptides, such as yeast pheromones, are often challenging. We developed a highly sensitive and robust affinity-assay for the quantification of the α-factor pheromone of Saccharomyces cerevisiae based on recombinant hydrophobins. These small, amphipathic proteins self-assemble into highly stable monolayers at hydrophilic-hydrophobic interfaces. Upon functionalization of solid supports with a combination of hydrophobins either lacking or exposing the α-factor, pheromone-specific antibodies were bound to the surface. Increasing concentrations of the pheromone competitively detached the antibodies, thus allowing for quantification of the pheromone. By adjusting the percentage of pheromone-exposing hydrophobins, the sensitivity of the assay could be precisely predefined. The assay proved to be highly robust against changes in sample matrix composition. Due to the high stability of hydrophobin layers, the functionalized surfaces could be repeatedly used without affecting the sensitivity. Furthermore, by using an inverse setup, the sensitivity was increased by three orders of magnitude, yielding a novel kind of biosensor for the yeast pheromone with the lowest limit of detection reported so far. This assay was applied to study the pheromone secretion of diverse yeast strains including a whole-cell biosensor strain of Schizosaccharomyces pombe modulating α-factor secretion in response to an environmental signal., Analyt-Detektion, Hefepheromon, Hydrophobin, Oberflächenfunktionalisierung, Vollzell-Biosensor, Biosensor, Analyte Detection, Yeast Pheromone, Surface Functionalization, Whole-Cell Biosensor, Rödel, Gerhard, Ostermann, Kai, Sensors (2016), 16(5), ISSN 1424-8220. DOI: 10.3390/s16050602. Artikelnr.: 602, text/html https://nbn-resolving.org/urn:nbn:de:bsz:14-qucosa-214807 Online-Zugriff |
| spellingShingle |
Hennig, Stefan, Hydrophobin-Based Surface Engineering for Sensitive and Robust Quantification of Yeast Pheromones, Detection and quantification of small peptides, such as yeast pheromones, are often challenging. We developed a highly sensitive and robust affinity-assay for the quantification of the α-factor pheromone of Saccharomyces cerevisiae based on recombinant hydrophobins. These small, amphipathic proteins self-assemble into highly stable monolayers at hydrophilic-hydrophobic interfaces. Upon functionalization of solid supports with a combination of hydrophobins either lacking or exposing the α-factor, pheromone-specific antibodies were bound to the surface. Increasing concentrations of the pheromone competitively detached the antibodies, thus allowing for quantification of the pheromone. By adjusting the percentage of pheromone-exposing hydrophobins, the sensitivity of the assay could be precisely predefined. The assay proved to be highly robust against changes in sample matrix composition. Due to the high stability of hydrophobin layers, the functionalized surfaces could be repeatedly used without affecting the sensitivity. Furthermore, by using an inverse setup, the sensitivity was increased by three orders of magnitude, yielding a novel kind of biosensor for the yeast pheromone with the lowest limit of detection reported so far. This assay was applied to study the pheromone secretion of diverse yeast strains including a whole-cell biosensor strain of Schizosaccharomyces pombe modulating α-factor secretion in response to an environmental signal., Analyt-Detektion, Hefepheromon, Hydrophobin, Oberflächenfunktionalisierung, Vollzell-Biosensor, Biosensor, Analyte Detection, Yeast Pheromone, Surface Functionalization, Whole-Cell Biosensor |
| title |
Hydrophobin-Based Surface Engineering for Sensitive and Robust Quantification of Yeast Pheromones |
| title_auth |
Hydrophobin-Based Surface Engineering for Sensitive and Robust Quantification of Yeast Pheromones |
| title_full |
Hydrophobin-Based Surface Engineering for Sensitive and Robust Quantification of Yeast Pheromones |
| title_fullStr |
Hydrophobin-Based Surface Engineering for Sensitive and Robust Quantification of Yeast Pheromones |
| title_full_unstemmed |
Hydrophobin-Based Surface Engineering for Sensitive and Robust Quantification of Yeast Pheromones |
| title_in_hierarchy |
|
| title_short |
Hydrophobin-Based Surface Engineering for Sensitive and Robust Quantification of Yeast Pheromones |
| title_sort |
hydrophobin-based surface engineering for sensitive and robust quantification of yeast pheromones |
| title_unstemmed |
Hydrophobin-Based Surface Engineering for Sensitive and Robust Quantification of Yeast Pheromones |
| topic |
Analyt-Detektion, Hefepheromon, Hydrophobin, Oberflächenfunktionalisierung, Vollzell-Biosensor, Biosensor, Analyte Detection, Yeast Pheromone, Surface Functionalization, Whole-Cell Biosensor |
| topic_facet |
Analyt-Detektion, Hefepheromon, Hydrophobin, Oberflächenfunktionalisierung, Vollzell-Biosensor, Biosensor, Analyte Detection, Yeast Pheromone, Surface Functionalization, Whole-Cell Biosensor |
| url |
https://nbn-resolving.org/urn:nbn:de:bsz:14-qucosa-214807 |
| urn |
urn:nbn:de:bsz:14-qucosa-214807 |
| work_keys_str_mv |
AT hennigstefan hydrophobinbasedsurfaceengineeringforsensitiveandrobustquantificationofyeastpheromones, AT rodelgerhard hydrophobinbasedsurfaceengineeringforsensitiveandrobustquantificationofyeastpheromones, AT ostermannkai hydrophobinbasedsurfaceengineeringforsensitiveandrobustquantificationofyeastpheromones |
