% 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{Engelberg:475051,
      author       = {Engelberg, Yizhaq and Ragonis-Bachar, Peleg and Landau,
                      Meytal},
      title        = {{R}are by {N}atural {S}election: {D}isulfide-{B}onded
                      {S}upramolecular {A}ntimicrobial {P}eptides},
      journal      = {Biomacromolecules},
      volume       = {23},
      number       = {3},
      issn         = {1525-7797},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Soc.},
      reportid     = {PUBDB-2022-01162},
      pages        = {926 – 936},
      year         = {2022},
      abstract     = {Human LL-37$_{17–29}$ is an antimicrobial peptide forming
                      thermostable supramolecular fibrils that surround bacterial
                      cells. The crystal structure of LL-37$_{17–29}$ bearing an
                      I24C substitution of most buried position in the fibril
                      revealed disulfide-bonded dimers that further assembled into
                      a fibrillar structure of densely packed helices. We further
                      demonstrated the position-dependent controllable
                      antibacterial activity of LL-37$_{17–29}$ I24C and other
                      cysteine mutants, mediated by regulation of intermolecular
                      disulfide bonds and their role in the formation of
                      supramolecular structures. The morphology of the fibrils and
                      their antibacterial mechanism of action might be dependent
                      on their interactions with specific bacteria. The
                      significant effect of disulfide bonds on the assembly into
                      supramolecular structures and their sensitivity to
                      reducing/oxidizing conditions may explain why short helical
                      antimicrobial peptides with a single cysteine and an odd
                      number of cysteines are selected against in nature.},
      cin          = {CSSB-F / EMBL-User},
      ddc          = {570},
      cid          = {I:(DE-H253)CSSB-F-20230420 / I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {35061360},
      UT           = {WOS:000813069600001},
      doi          = {10.1021/acs.biomac.1c01353},
      url          = {https://bib-pubdb1.desy.de/record/475051},
}