@article{BanKaračićTomićetal.2021,
  author    = {Ban, Željka and Karačić, Zrinka and Tomić, Sanja and Amini, Hashem and Marder, Todd B. and Piantanida, Ivo},
  title     = {Triarylborane dyes as a novel non-covalent and non-inhibitive fluorimetric markers for DPP III enzyme},
  series = {Molecules},
  volume    = {26},
  journal   = {Molecules},
  number    = {16},
  issn      = {1420-3049},
  doi       = {10.3390/molecules26164816},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-245046},
  year      = {2021},
  abstract  = {Novel dyes were prepared by simple "click CuAAC" attachment of a triarylborane-alkyne to the azide side chain of an amino acid yielding triarylborane dye 1 which was conjugated with pyrene (dye 2) forming a triarylborane-pyrene FRET pair. In contrast to previous cationic triarylboranes, the novel neutral dyes interact only with proteins, while their affinity to DNA/RNA is completely abolished. Both the reference triarylborane amino acid and triarylborane-pyrene conjugate bind to BSA and the hDPP III enzyme with high affinities, exhibiting a strong (up to 100-fold) fluorescence increase, whereby the triarylborane-pyrene conjugate additionally retained FRET upon binding to the protein. Furthermore, the triarylborane dyes, upon binding to the hDPP III enzyme, did not impair its enzymatic activity under a wide range of experimental conditions, thus being the first non-covalent fluorimetric markers for hDPP III, also applicable during enzymatic reactions with hDPP III substrates.},
  language  = {en}
}