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@ARTICLE{Gao:839931,
      author       = {Gao, Jie and Tang, Claire and Elsawy, Mohamed A. and Smith,
                      Andrew M. and Miller, Aline F. and Saiani, Alberto},
      title        = {{C}ontrolling {S}elf-{A}ssembling {P}eptide {H}ydrogel
                      {P}roperties through {N}etwork {T}opology},
      journal      = {Biomacromolecules},
      volume       = {18},
      number       = {3},
      issn         = {1526-4602},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Soc.},
      reportid     = {FZJ-2017-07509},
      pages        = {826 - 834},
      year         = {2017},
      abstract     = {Self-assembling peptide-based hydrogels have encountered
                      increasing interest in the recent years as scaffolds for 3D
                      cell culture or for controlled drug delivery. One of the
                      main challenges is the fine control of the mechanical
                      properties of these materials. The bulk properties of
                      hydrogels not only depend on the intrinsic properties of the
                      fibers but also on the network topology formed. In this work
                      we show how fiber–fiber interactions can be manipulated by
                      design to control the final hydrogel network topology and
                      therefore control the final properties of the material. This
                      was achieved by exploiting the design features of β-sheet
                      forming peptides based on hydrophobic and hydrophilic
                      residue alternation and exploiting the ability of the
                      arginine’s guanidine side group to interact with itself
                      and with other amino acid side groups. By designing
                      octa-peptides based on phenylalanine, glutamic acid, lysine,
                      and arginine, we have investigated how fiber association and
                      bundling affect the dynamic shear modulus of hydrogels and
                      how it can be controlled by design. This work opens the
                      possibility to fine-tune by design the bulk properties of
                      peptide hydrogels.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6G15 - FRM II / MLZ (POF3-6G15)},
      pid          = {G:(DE-HGF)POF3-6G4 / G:(DE-HGF)POF3-6G15},
      experiment   = {EXP:(DE-MLZ)KWS2-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:28068466},
      UT           = {WOS:000396379600017},
      doi          = {10.1021/acs.biomac.6b01693},
      url          = {https://juser.fz-juelich.de/record/839931},
}