@article{HoangHaubitzKumke2018,
  author    = {Hoang, Hoa T. and Haubitz, Toni and Kumke, Michael Uwe},
  title     = {Photophysics of "Floppy" Dyadsas Potential Biomembrane Probes},
  series = {Journal of fluorescence},
  volume    = {28},
  journal   = {Journal of fluorescence},
  number    = {5},
  publisher = {Springer},
  address   = {New York},
  issn      = {1053-0509},
  doi       = {10.1007/s10895-018-2286-4},
  pages     = {1225 -- 1237},
  year      = {2018},
  abstract  = {In the study a dyad (C6 probe), constructed of two dyes with highly different hydrophobicities, was investigated by steady-state and time-resolved spectroscopic techniques in chloroform, methanol, and in phospholipid vesicles, respectively. The dyad was built on two dyes: the lipophilic benzo[a]pyrene (BaP) and the hydrophilic sulforhodamine B (SRB). The dyes were linked via a short, but flexible alkyl chain (six C-atoms). Based on their spectroscopic properties, BaP and SRB showed a very efficient non-radiative resonance energy transfer in solution. Incorporation into a lipid bilayer limited the relative flexibility (degree of freedom) between donor and acceptor and was used for the investigation of fundamental photophysical aspects (especially of FRET) as well as to elucidate the potential of the dyad to probe the interface of vesicles (or cells). The location of the two dyes in vesicles and their respective accessibility for interactions with dye-specific antibodies was investigated. Based on the alteration of the anisotropy, on the rotational correlation time as well as on the diffusion coefficient the incorporation of the C6 probe into the vesicles was evaluated. Especially the limitation in the relative movements of the two dyes was considered and used to differentiate between potential parameters, that influence the energy transfer in the dyad. Transient absorption spectroscopy (TAS) and pulsed-interleave single molecule fluorescence experiments were performed to better understand the intramolecular interactions in the dyad. Finally, in a showcase for a biosensing application of the dyads, the binding of an SRB-specific antibody was investigated when the dyad was incorporated in vesicles.},
  language  = {en}
}
@article{EisoldSellrieSchenketal.2015,
  author    = {Eisold, Ursula and Sellrie, Frank and Schenk, J{\"o}rg A. and Lenz, Christine and St{\"o}cklein, Walter F. M. and Kumke, Michael Uwe},
  title     = {Bright or dark immune complexes of anti-TAMRA antibodies for adapted fluorescence-based bioanalysis},
  series = {Analytical \& bioanalytical chemistry},
  volume    = {407},
  journal   = {Analytical \& bioanalytical chemistry},
  number    = {12},
  publisher = {Springer},
  address   = {Heidelberg},
  issn      = {1618-2642},
  doi       = {10.1007/s00216-015-8538-0},
  pages     = {3313 -- 3323},
  year      = {2015},
  abstract  = {Fluorescence labels, for example fluorescein or rhodamin derivatives, are widely used in bioanalysis applications including lateral-flow assays, PCR, and fluorescence microscopy. Depending on the layout of the particular application, fluorescence quenching or enhancement may be desired as the detection principle. Especially for multiplexed applications or high-brightness requirements, a tunable fluorescence probe can be beneficial. The alterations in the photophysics of rhodamine derivatives upon binding to two different anti-TAMRA antibodies were investigated by absorption and fluorescence-spectroscopy techniques, especially determining the fluorescence decay time and steady-state and time-resolved fluorescence anisotropy. Two monoclonal anti-TAMRA antibodies were generated by the hybridoma technique. Although surface-plasmon-resonance measurements clearly proved the high affinity of both antibodies towards 5-TAMRA, the observed effects on the fluorescence of rhodamine derivatives were very different. Depending on the anti-TAMRA antibody either a strong fluorescence quenching (G71-DC7) or a distinct fluorescence enhancement (G71-BE11) upon formation of the immune complex was observed. Additional rhodamine derivatives were used to gain further information on the binding interaction. The data reveal that such haptens as 5-TAMRA could generate different paratopes with equal binding affinities but different binding interactions, which provide the opportunity to adapt bioanalysis methods including immunoassays for optimized detection principles for the same hapten depending on the specific requirements.},
  language  = {en}
}