Surfactant protein C peptides with salt-bridges (“ion-locks”) promote high surfactant activities by mimicking the α-helix and membrane topography of the native protein

Surfactant protein C peptides with salt-bridges (“ion-locks”) promote high surfactant activities by mimicking the α-helix and membrane topography of the native protein

Background. Surfactant protein C (SP-C; 35 residues) in lungs has a cationic N-terminal domain with two cysteines covalently linked to palmitoyls and a C-terminal region enriched in Val, Leu and Ile. Native SP-C shows high surface activity, due to SP-C inserting in the bilayer with its cationic N-te...

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Bibliographic Details
Main Authors: Frans J. Walther, Alan J. Waring, José M. Hernández-Juviel, Piotr Ruchala, Zhengdong Wang, Robert H. Notter, Larry M. Gordon
Format: Article
Language:English
Published: PeerJ Inc. 2014-07-01
Series:PeerJ
Subjects:
Protein synthesis
PASTA algorithm
Synthetic surfactant
Salt-bridges
Fourier Transform InfraRed spectroscopy
Membrane protein explorer program
Online Access:https://peerj.com/articles/485.pdf

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https://peerj.com/articles/485.pdf

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