Helical peptoid mimics of lung surfactant protein C.
Among the families of peptidomimetic foldamers under development as novel biomaterials and therapeutics, poly-N-substituted glycines (peptoids) with alpha-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.
Wu
Cindy W
CW
Department of Chemical Engineering, Northwestern University, 2145 Sheridan Road, Room E136, Evanston, IL 60208, USA.
Seurynck
Shannon L
SL
Lee
Ka Yee C
KY
Barron
Annelise E
AE
D002942:Circular Dichroism; D008856:Microscopy, Fluorescence; D008958:Models, Molecular; D018716:Molecular Mimicry; D017433:Protein Structure, Secondary; D037721:Pulmonary Surfactant-Associated Protein C / Q000737:chemistry*
D037721:Pulmonary Surfactant-Associated Protein C