% 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{Segal:329294,
      author       = {Segal, Merav and Avinery, Ram and Buzhor, Marina and
                      Shaharabani, Rona and Harnoy, Assaf J. and Tirosh, Einat and
                      Beck, Roy and Amir, Roey J.},
      title        = {{M}olecular {P}recision and {E}nzymatic {D}egradation:
                      {F}rom {R}eadily to {U}ndegradable {P}olymeric {M}icelles by
                      {M}inor {S}tructural {C}hanges},
      journal      = {Journal of the American Chemical Society},
      volume       = {139},
      number       = {2},
      issn         = {1520-5126},
      address      = {Washington, DC},
      publisher    = {American Chemical Society},
      reportid     = {PUBDB-2017-05909},
      pages        = {803 - 810},
      year         = {2017},
      abstract     = {Studying the enzymatic degradation of synthetic polymers is
                      crucial for the design of suitable materials for biomedical
                      applications ranging from advanced drug delivery systems to
                      tissue engineering. One of the key parameters that governs
                      enzymatic activity is the limited accessibility of the
                      enzyme to its substrates that may be collapsed inside
                      hydrophobic domains. PEG-dendron amphiphiles can serve as
                      powerful tools for the study of enzymatic hydrolysis of
                      polymeric amphiphiles due to the monodispersity and symmetry
                      of the hydrophobic dendritic block, which significantly
                      simplifies kinetic analyses. Using these hybrids, we
                      demonstrate how precise, minor changes in the hydrophobic
                      block are manifested into tremendous changes in the
                      stability of the assembled micelles toward enzymatic
                      degradation. The obtained results emphasize the extreme
                      sensitivity of self-assembly and its great importance in
                      regulating the accessibility of enzymes to their substrates.
                      Furthermore, the demonstration that the structural
                      differences between readily degradable and undegradable
                      micelles are rather minor, points to the critical roles that
                      self-assembly and polydispersity play in designing
                      biodegradable materials.},
      cin          = {EMBL / EMBL-User},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-20120731 / I:(DE-H253)EMBL-User-20120814},
      pnm          = {BIOSTRUCT-X - Transnational access and enhancement of
                      integrated Biological Structure determination at synchrotron
                      X-ray radiation facilities (283570) / 6G3 - PETRA III
                      (POF3-622)},
      pid          = {G:(EU-Grant)283570 / G:(DE-HGF)POF3-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000392459300039},
      pubmed       = {pmid:27990807},
      doi          = {10.1021/jacs.6b10624},
      url          = {https://bib-pubdb1.desy.de/record/329294},
}