% 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{Xu:614232,
      author       = {Xu, Maokai and Antonova, Maria and Salavei, Pavel and
                      Illek, Katharina and Meléndez, Ana Valeria and Omidvar,
                      Ramin and Thuenauer, Roland and Makshakova, Olga and Roemer,
                      Winfried},
      title        = {{D}imeric {L}ectin {C}himeras as {N}ovel {C}andidates for
                      {G}b3-{M}ediated {T}ranscytotic {D}rug {D}elivery through
                      {C}ellular {B}arriers},
      journal      = {Pharmaceutics},
      volume       = {15},
      number       = {1},
      issn         = {1999-4923},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {PUBDB-2024-05772},
      pages        = {225},
      year         = {2023},
      abstract     = {Receptor-mediated transcytosis is an elegant and promising
                      strategy for drug delivery across biological barriers. Here,
                      we describe a novel ligand–receptor pair based on a
                      dimeric, engineered derivative of the Pseudomonas aeruginosa
                      lectin LecA, here termed Di-LecA, and the host cell
                      glycosphingolipid Gb3. We characterized the trafficking
                      kinetics and transcytosis efficiencies in polarized
                      Gb3-positive and -negative MDCK cells using mainly
                      immunofluorescence in combination with confocal microscopy.
                      To evaluate the delivery capacity of dimeric LecA chimeras,
                      EGFP was chosen as a fluorescent model protein representing
                      macromolecules, such as antibody fragments, and fused to
                      either the N- or C-terminus of monomeric LecA using
                      recombinant DNA technology. Both LecA/EGFP fusion proteins
                      crossed cellular monolayers in vitro. Of note, the conjugate
                      with EGFP at the N-terminus of LecA (EGFP-LecA) showed a
                      higher release rate than the conjugate with EGFP at the
                      C-terminus (LecA-EGFP). Based on molecular dynamics
                      simulations and cross-linking studies of giant unilamellar
                      vesicles, we speculate that EGFP-LecA tends to be a dimer
                      while LecA-EGFP forms a tetramer. Overall, we confidently
                      propose the dimeric LecA chimeras as transcytotic drug
                      delivery tools through Gb3-positive cellular barriers for
                      future in vivo tests.Keywords:Gb3-binding lectin;
                      glycosphingolipid; transcytosis; drug carrier; protein
                      engineering; protein structure; valency; accelerated
                      molecular dynamics},
      cin          = {CSSB-CF-ALFM},
      ddc          = {610},
      cid          = {I:(DE-H253)CSSB-CF-ALFM-20210629},
      pnm          = {899 - ohne Topic (POF4-899) / DFG project
                      G:(GEPRIS)39236281 - EXC 294: BIOSS Zentrum für Biologische
                      Signalstudien - von der Analyse zur Synthese (39236281) /
                      DFG project G:(GEPRIS)390939984 - EXC 2189: CIBSS - Centre
                      for Integrative Biological Signalling Studies (390939984)},
      pid          = {G:(DE-HGF)POF4-899 / G:(GEPRIS)39236281 /
                      G:(GEPRIS)390939984},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:36678854},
      UT           = {WOS:000918781700001},
      doi          = {10.3390/pharmaceutics15010225},
      url          = {https://bib-pubdb1.desy.de/record/614232},
}