10.1021/acsami.7b01587.s001
Shanshan Wang
Shanshan
Wang
Charles J. Zeman
Charles J.
Zeman
Junlin Jiang
Junlin
Jiang
Zhenxing Pan
Zhenxing
Pan
Kirk S. Schanze
Kirk S.
Schanze
Intercalation
of Alkynylplatinum(II) Terpyridine Complexes
into a Helical Poly(phenylene ethynylene) Sulfonate: Application to
Protein Sensing
American Chemical Society
2017
PPESO
sulfonate-conjugated polyelectrolytes
Pt
polymer helix
3 MMLCT
3 MMLCT state emission
state emission
protein
complex
ensemble
fluorescence
2017-04-11 12:48:29
Journal contribution
https://acs.figshare.com/articles/journal_contribution/Intercalation_of_Alkynylplatinum_II_Terpyridine_Complexes_into_a_Helical_Poly_phenylene_ethynylene_Sulfonate_Application_to_Protein_Sensing/4854662
The
interactions of two anionic poly(phenylene ethynylene) sulfonate-conjugated
polyelectrolytes (<i>m</i>PPESO<sub>3</sub><sup>–</sup> and <i>p</i>PPESO<sub>3</sub><sup>–</sup>) with
two alkynylplatinum(II) terpyridine complexes (Pt<sup>2+</sup> and
Pt<sup>3+</sup>) were studied. The Pt(II) complexes interact with
helical <i>m</i>PPESO<sub>3</sub><sup>–</sup> by
intercalation within the polymer helix to form a “guest–host”
ensemble. Titration of Pt(II) complexes into an aqueous solution of <i>m</i>PPESO<sub>3</sub><sup>–</sup> gives rise to efficient
quenching of the polymer’s fluorescence; meanwhile, triplet
metal–metal-to-ligand charge transfer (<sup>3</sup>MMLCT) state
emission from the intercalated Pt(II) complexes appears when the ensembles
are excited into the polymer’s absorption band. The <sup>3</sup>MMLCT state emission implies that the Pt(II) complexes aggregate
or dimerize on the <i>m</i>PPESO<sub>3</sub><sup>–</sup> scaffold. The responses of the <i>m</i>PPESO<sub>3</sub><sup>–</sup> and Pt(II) complex ensembles to various proteins
were examined by monitoring the <i>m</i>PPESO<sub>3</sub><sup>–</sup> fluorescence change. Negatively charged proteins
recover the <i>m</i>PPESO<sub>3</sub><sup>–</sup> fluorescence more than the positively charged proteins under physiological
pH, indicating that electrostatics play an important role in the protein–ensemble
interaction.