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@ARTICLE{McDaniel:171844,
      author       = {McDaniel, Jonathan R. and Weitzhandler, Isaac and Prevost,
                      Sylvain and Vargo, Kevin B. and Appavou, Marie-Sousai and
                      Hammer, Daniel A. and Gradzielski, Michael and Chilkoti,
                      Ashutosh},
      title        = {{N}oncanonical {S}elf-{A}ssembly of {H}ighly {A}symmetric
                      {G}enetically {E}ncoded {P}olypeptide {A}mphiphiles into
                      {C}ylindrical {M}icelles},
      journal      = {Nano letters},
      volume       = {14},
      number       = {11},
      issn         = {1530-6992},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {FZJ-2014-05401},
      pages        = {6590–6598},
      year         = {2014},
      abstract     = {Elastin-like polypeptides (ELPs) are a class of biopolymers
                      consisting of the pentameric repeat (VPGαG)n based on the
                      sequence of mammalian tropoelastin that display a thermally
                      induced soluble-to-insoluble phase transition in aqueous
                      solution. We have discovered a remarkably simple approach to
                      driving the spontaneous self-assembly of high molecular
                      weight ELPs into nanostructures by genetically fusing a
                      short 1.5 kDa (XGy)z assembly domain to one end of the ELP.
                      Classical theories of self-assembly based on the geometric
                      mass balance of hydrophilic and hydrophobic block copolymers
                      suggest that these highly asymmetric polypeptides should
                      form spherical micelles. Surprisingly, when sufficiently
                      hydrophobic amino acids (X) are presented in a periodic
                      sequence such as (FGG)8 or (YG)8, these highly asymmetric
                      polypeptides self-assemble into cylindrical micelles whose
                      length can be tuned by the sequence of the morphogenic tag.
                      These nanostructures were characterized by light scattering,
                      tunable resistive pulse sensing, fluorescence
                      spectrophotometry, and thermal turbidimetry, as well as by
                      cryogenic transmission electron microscopy (cryo-TEM) and
                      small-angle neutron scattering (SANS). These short assembly
                      domains provide a facile strategy to control the size,
                      shape, and stability of stimuli responsive polypeptide
                      nanostructures.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218},
      pnm          = {54G - JCNS (POF2-54G24)},
      pid          = {G:(DE-HGF)POF2-54G24},
      experiment   = {EXP:(DE-MLZ)KWS3-20140101 / EXP:(DE-MLZ)KWS1-20140101 /
                      EXP:(DE-MLZ)KWS2-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000345723800089},
      pubmed       = {pmid:25268037},
      doi          = {10.1021/nl503221p},
      url          = {https://juser.fz-juelich.de/record/171844},
}