{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Walther FJ"],"funding":["NIEHS NIH HHS","NHLBI NIH HHS"],"pagination":["e485"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4106191"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["2"],"pubmed_abstract":["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-terminus binding to the polar headgroup and its hydrophobic C-terminus embedded as a tilted, transmembrane α-helix. The palmitoylcysteines in SP-C act as 'helical adjuvants' to maintain activity by overriding the β-sheet propensities of the native sequences. Objective. We studied SP-C peptides lacking palmitoyls, but containing glutamate and lysine at 4-residue intervals, to assess whether SP-C peptides with salt-bridges (\"ion-locks\") promote surface activity by mimicking the α-helix and membrane "],"journal":["PeerJ"],"pubmed_title":["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."],"pmcid":["PMC4106191"],"funding_grant_id":["R01 ES015330","R01 HL092158","R01 HL094641"],"pubmed_authors":["Walther FJ","Hernandez-Juviel JM","Ruchala P","Waring AJ","Notter RH","Wang Z","Gordon LM"],"additional_accession":[]},"is_claimable":false,"name":"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.","description":"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-terminus binding to the polar headgroup and its hydrophobic C-terminus embedded as a tilted, transmembrane α-helix. The palmitoylcysteines in SP-C act as 'helical adjuvants' to maintain activity by overriding the β-sheet propensities of the native sequences. Objective. We studied SP-C peptides lacking palmitoyls, but containing glutamate and lysine at 4-residue intervals, to assess whether SP-C peptides with salt-bridges (\"ion-locks\") promote surface activity by mimicking the α-helix and membrane ","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014","modification":"2025-04-18T15:06:12.053Z","creation":"2019-03-27T01:32:31Z"},"accession":"S-EPMC4106191","cross_references":{"pubmed":["25083348"],"doi":["10.7717/peerj.485"]}}