Distyrylbenzene-aldehydes: identification of proteins in water
Three different, water soluble, aldehyde-appended distyrylbenzene (DSB) derivatives were prepared. Their interaction with different albumin variants (human, porcine, bovine, lactalbumin, ovalbumin) was investigated (pH 11). All three fluorophores exhibit graded, protein-dependent fluorescence turn-o...
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| Hauptverfasser: | , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
12 Mar 2015
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| In: |
The analyst
Year: 2015, Jahrgang: 140, Heft: 9, Pages: 3136-3142 |
| ISSN: | 1364-5528 |
| DOI: | 10.1039/C5AN00155B |
| Online-Zugang: | Resolving-System, lizenzpflichtig, Volltext: https://doi.org/10.1039/C5AN00155B Verlag, lizenzpflichtig, Volltext: https://pubs.rsc.org/en/content/articlelanding/2015/an/c5an00155b 
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| Verfasserangaben: | Jan Kumpf, Jan Freudenberg and Uwe H.F. Bunz |
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| 520 | |a Three different, water soluble, aldehyde-appended distyrylbenzene (DSB) derivatives were prepared. Their interaction with different albumin variants (human, porcine, bovine, lactalbumin, ovalbumin) was investigated (pH 11). All three fluorophores exhibit graded, protein-dependent fluorescence turn-on at slightly differing wavelengths. Linear discriminant analysis (LDA) differentiated all of the investigated albumins and was used to discern commercially available protein shakes. The three DSB derivatives barely react with the constituting amino acids but cysteine. In the proteins significant fluorescence signals are generated, probably due to a combination of imine/N,S-aminal formation and hydrophobic interactions between the DSBs and the proteins. | ||
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