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@ARTICLE{Neuhaus:273920,
      author       = {Neuhaus, Charlotte and Alfken, Jette and Frost, Jakob and
                      Matthews, Lauren and Hoffmann, Christian and Ganzella,
                      Marcelo and Milovanovic, Dragomir and Salditt, Tim},
      title        = {{M}orphology and intervesicle distances in condensates of
                      synaptic vesicles and synapsin.},
      journal      = {Biophysical journal},
      volume       = {123},
      number       = {23},
      issn         = {0006-3495},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {DZNE-2024-01394},
      pages        = {4123 - 4134},
      year         = {2024},
      abstract     = {Synaptic vesicle clusters or pools are functionally
                      important constituents of chemical synapses. In the
                      so-called reserve and the active pools,
                      neurotransmitter-loaded synaptic vesicles (SVs) are stored
                      and conditioned for fusion with the synaptic membrane and
                      subsequent neurotransmitter release during synaptic
                      activity. Vesicle clusters can be considered as so-called
                      membraneless compartments, which form by liquid-liquid phase
                      separation. Synapsin as one of the most abundant synaptic
                      proteins has been identified as a major driver of pool
                      formation. It has been shown to induce liquid-liquid phase
                      separation and form condensates on its own in solution, but
                      also has been shown to integrate vesicles into condensates
                      in vitro. In this process, the intrinsically disordered
                      region of synapsin is believed to play a critical role.
                      Here, we first investigate the solution structure of
                      synapsin and SVs separately by small-angle x-ray scattering.
                      In the limit of low momentum transfer q, the scattering
                      curve for synapsin gives clear indication for supramolecular
                      aggregation (condensation). We then study mixtures of SVs
                      and synapsin-forming condensates, aiming at the morphology
                      and intervesicle distances, i.e., the structure of the
                      condensates in solution. To obtain the structure factor S(q)
                      quantifying intervesicle correlation, we divide the
                      scattering curve of condensates by that of pure SV
                      suspensions. Analysis of S(q) in combination with numerical
                      simulations of cluster aggregation indicates a noncompact
                      fractal-like vesicular fluid with rather short intervesicle
                      distances at the contact sites.},
      keywords     = {Synapsins: metabolism / Synapsins: chemistry / Synaptic
                      Vesicles: metabolism / Synaptic Vesicles: chemistry /
                      Animals / Scattering, Small Angle / X-Ray Diffraction / Rats
                      / Biomolecular Condensates: chemistry / Biomolecular
                      Condensates: metabolism / Synapsins (NLM Chemicals)},
      cin          = {AG Milovanovic (Berlin)},
      ddc          = {570},
      cid          = {I:(DE-2719)1813002},
      pnm          = {351 - Brain Function (POF4-351)},
      pid          = {G:(DE-HGF)POF4-351},
      typ          = {PUB:(DE-HGF)16},
      pmc          = {pmc:PMC11628805},
      pubmed       = {pmid:39520054},
      doi          = {10.1016/j.bpj.2024.11.004},
      url          = {https://pub.dzne.de/record/273920},
}