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- W2032853605 abstract "Among the families of peptidomimetic foldamers under development as novel biomaterials and therapeutics, poly-N-substituted glycines (peptoids) with α-chiral side chains are of particular interest for their ability to adopt stable, helical secondary structure in organic and aqueous solution. Here, we show that a peptoid 22-mer with a biomimetic sequence of side chains and an amphipathic, helical secondary structure acts as an excellent mimic of surfactant protein C (SP-C), a small protein that plays an important role in surfactant replacement therapy for the treatment of neonatal respiratory distress syndrome. When integrated into a lipid film, the helical peptoid SP mimic captures the essential surface-active behaviors of the natural protein. This work provides an example of how an abiological oligomer that closely mimics both the hydrophobic/polar sequence patterning and the fold of a natural protein can also mimic its biophysical function." @default.
- W2032853605 created "2016-06-24" @default.
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- W2032853605 date "2003-11-01" @default.
- W2032853605 modified "2023-10-16" @default.
- W2032853605 title "Helical Peptoid Mimics of Lung Surfactant Protein C" @default.
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- W2032853605 doi "https://doi.org/10.1016/j.chembiol.2003.10.008" @default.
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