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231225s2020 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.0c01328
|2 doi
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|a pubmed24n1035.xml
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|a (DE-627)NLM310805805
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|a (NLM)32501009
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Robert, Bruno
|e verfasserin
|4 aut
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| 245 |
1 |
0 |
|a Strategies for Chalcogenide Thin Film Functionalization
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| 264 |
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|c 2020
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| 336 |
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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| 500 |
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|a Date Completed 09.09.2020
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|a Date Revised 09.09.2020
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|a published: Print-Electronic
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|a Citation Status PubMed-not-MEDLINE
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|a We report the functionalization of chalcogenide thin films with biotinylated 12-mer peptides SVSVGMKPSPRP and LLADTTHHRPWT exhibiting a high binding affinity toward inorganic surfaces, on the one hand, and with (3-aminopropyl)triethoxysilane (APTES), on the other hand. The specific biotin moieties were used to bind streptavidin proteins and demonstrate the efficacy of the biofunctionalizated chalcogenide thin films to capture biomolecules. Atomic force microscopy provided high-resolution images of the interfaces, and water contact angle measurements gave insight into the interaction mechanisms. Fourier transform infrared spectroscopy in attenuated total reflection mode provided information about the secondary structure of the bound proteins, thanks to the deconvolution of the amide I band (1700-1600 cm-1). Following adsorption of the biotinylated peptides or APTES immobilization, a homogenous coverage of the biotin layer exhibiting very low roughness was obtained, also rendering more hydrophilic Ge-Se-Te surfaces. Subsequent capture of streptavidin depends on the functionalization approach, permitting more or less an optimal orientation of the biotin to bind streptavidin. The molecular interface layer formed on Ge-Se-Te is crucial also for retaining the native secondary structure of the protein. Altogether, our results demonstrate that both peptides and APTES were appropriate linkers to build a favorable interface on chalcogenide materials to capture proteins, opening hereby promising biosensing applications
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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1 |
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|a Martin, Marta
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Escalier, Raphaël
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Varga, Béla
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Mehdi, Ahmad
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Vigreux, Caroline
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Gergely, Csilla
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 36(2020), 26 vom: 07. Juli, Seite 7691-7700
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
1 |
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|g volume:36
|g year:2020
|g number:26
|g day:07
|g month:07
|g pages:7691-7700
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|u http://dx.doi.org/10.1021/acs.langmuir.0c01328
|3 Volltext
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