% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Ruks:891697,
      author       = {Ruks, Tatjana and Loza, Kateryna and Heggen, Marc and
                      Prymak, Oleg and Sehnem, Andre Luiz and Oliveira, Cristiano
                      L. P. and Bayer, Peter and Beuck, Christine and Epple,
                      Matthias},
      title        = {{P}eptide-{C}onjugated {U}ltrasmall {G}old {N}anoparticles
                      (2 nm) for {S}elective {P}rotein {T}argeting},
      journal      = {ACS applied bio materials},
      volume       = {4},
      number       = {1},
      issn         = {2576-6422},
      address      = {Washington, DC},
      publisher    = {ACS Publications},
      reportid     = {FZJ-2021-01676},
      pages        = {945 - 965},
      year         = {2021},
      abstract     = {Ultrasmall gold nanoparticles with a metallic core diameter
                      of 2 nm were surface-conjugated with peptides that
                      selectively target epitopes on the surface of the WW domain
                      of the model protein hPin1 (hPin1-WW). The binding to the
                      gold surface was accomplished via the thiol group of a
                      terminal cysteine. The particles were analyzed by NMR
                      spectroscopy, high-resolution transmission electron
                      microscopy, and differential centrifugal sedimentation. The
                      surface loading was determined by conjugating a FAM-labeled
                      peptide, followed by UV–vis spectroscopy, and by
                      quantitative 1H NMR spectroscopy, showing about 150 peptide
                      molecules conjugated to each nanoparticle. The interaction
                      between the peptide-decorated nanoparticles with hPin1-WW
                      was probed by 1H–15N-HSQC NMR titration, fluorescence
                      polarization spectroscopy (FP), and isothermal titration
                      calorimetry (ITC). The particles showed a similar binding
                      (KD = 10–20 μM) compared to the dissolved peptides (KD =
                      10–30 μM). Small-angle X-ray scattering (SAXS) showed
                      that the particles were well dispersed and did not
                      agglomerate after the addition of hPin1-WW (no cross-linking
                      by the protein). Each nanoparticle was able to bind about 20
                      hPin1-WW protein molecules. An unspecific interaction with
                      hPin1 was excluded by the attachment of a nonbinding peptide
                      to the nanoparticle surface. The uptake by cells was studied
                      by confocal laser scanning microscopy. The
                      peptide-functionalized nanoparticles penetrated the cell
                      membrane and were located in the cytosol. In contrast, the
                      dissolved peptide did not cross the cell membrane.
                      Peptide-functionalized nanoparticles are promising agents to
                      target proteins inside cells.},
      cin          = {ER-C-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ER-C-1-20170209},
      pnm          = {535 - Materials Information Discovery (POF4-535)},
      pid          = {G:(DE-HGF)POF4-535},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000643599900072},
      doi          = {10.1021/acsabm.0c01424},
      url          = {https://juser.fz-juelich.de/record/891697},
}