Effects of hydrophobic helix length and side chain chemistry on biomimicry in peptoid analogues of SP-C.

@article{Brown2008EffectsOH,
  title={Effects of hydrophobic helix length and side chain chemistry on biomimicry in peptoid analogues of SP-C.},
  author={Nathan J. Brown and Cindy W Wu and Shannon L Seurynck-Servoss and Annelise E. Barron},
  journal={Biochemistry},
  year={2008},
  volume={47 6},
  pages={1808-18}
}
The hydrophobic proteins of lung surfactant (LS), SP-B and SP-C, are critical constituents of an effective surfactant replacement therapy for the treatment of respiratory distress syndrome. Because of concerns and difficulties associated with animal-derived surfactants, recent investigations have focused on the creation of synthetic analogues of the LS proteins. However, creating an accurate mimic of SP-C that retains its biophysical surface activity is extraordinarily challenging given the… CONTINUE READING

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Synthetic mimetics of protein secondary structure domains

Philosophical transactions. Series A, Mathematical, physical, and engineering sciences • 2010
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Peptoid architectures: elaboration, actuation, and application.

Current opinion in chemical biology • 2008
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