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@ARTICLE{Mezgec:618994,
      author       = {Mezgec, Klemen and Snoj, Jaka and Ulčakar, Liza and
                      Ljubetič, Ajasja and Tušek Žnidarič, Magda and
                      Škarabot, Miha and Jerala, Roman},
      title        = {{C}oupling of {S}pectrin {R}epeat {M}odules for the
                      {A}ssembly of {N}anorods and {P}resentation of {P}rotein
                      {D}omains},
      journal      = {ACS nano},
      volume       = {18},
      number       = {42},
      issn         = {1936-0851},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {PUBDB-2024-07304},
      pages        = {28748-28763},
      year         = {2024},
      abstract     = {Modular protein engineering is a powerful approach for
                      fabricating high-molecular-weight assemblies and
                      biomaterials with nanoscale precision. Herein, we address
                      the challenge of designing an extended nanoscale filamentous
                      architecture inspired by the central rod domain of human
                      dystrophin, which protects sarcolemma during muscle
                      contraction and consists of spectrin repeats composed of
                      three-helical bundles. A module of three tandem spectrin
                      repeats was used as a rigid building block self-assembling
                      via coiled-coil (CC) dimer-forming peptides. CC peptides
                      were precisely integrated to maintain the spectrin α-helix
                      continuity in an appropriate frame to form extended
                      nanorods. An orthogonal set of customizable CC heterodimers
                      was harnessed for modular rigid domain association, which
                      could be additionally regulated by metal ions and chelators.
                      We achieved a robust assembly of rigid rods several
                      micrometers in length, determined by atomic force microscopy
                      and negative stain transmission electron microscopy.
                      Furthermore, these rigid rods can serve as a scaffold for
                      the decoration of diverse proteins or biologically active
                      peptides along their length with adjustable spacing up to
                      tens of nanometers, as confirmed by the DNA-PAINT
                      super-resolution microscopy. This demonstrates the potential
                      of modular bottom-up protein engineering and tunable CCs for
                      the fabrication of functionalized protein biomaterials.},
      cin          = {EMBL-User},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / CTGCT - Centre of
                      Excellence for the Technologies of Gene and Cell Therapy
                      (101059842) / LoopOfFun - Closed-loop control of fungal
                      materials (101070817) / VIROFIGHT - General-purpose
                      virus-neutralizing engulfing shells with modular
                      target-specificity (899619)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(EU-Grant)101059842 /
                      G:(EU-Grant)101070817 / G:(EU-Grant)899619},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39392430},
      UT           = {WOS:001338243200001},
      doi          = {10.1021/acsnano.4c07701},
      url          = {https://bib-pubdb1.desy.de/record/618994},
}