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- W4308045202 startingPage "e0276787" @default.
- W4308045202 abstract "The three-dimensional structure of the synthetic lung Surfactant Protein B Peptide Super Mini-B was determined using an integrative experimental approach, including mass spectrometry and isotope enhanced Fourier-transform infrared (FTIR) spectroscopy. Mass spectral analysis of the peptide, oxidized by solvent assisted region-specific disulfide formation, confirmed that the correct folding and disulfide pairing could be facilitated using two different oxidative structure-promoting solvent systems. Residue specific analysis by isotope enhanced FTIR indicated that the N-terminal and C-terminal domains have well defined α-helical amino acid sequences. Using these experimentally derived measures of distance constraints and disulfide connectivity, the ensemble was further refined with molecular dynamics to provide a medium resolution, residue-specific structure for the peptide construct in a simulated synthetic lung surfactant lipid multilayer environment. The disulfide connectivity combined with the α-helical elements stabilize the peptide conformationally to form a helical hairpin structure that resembles critical elements of the Saposin protein fold of the predicted full-length Surfactant Protein B structure." @default.
- W4308045202 created "2022-11-07" @default.
- W4308045202 creator A5012020338 @default.
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- W4308045202 creator A5060778334 @default.
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- W4308045202 date "2022-11-03" @default.
- W4308045202 modified "2023-10-16" @default.
- W4308045202 title "Emulation of the structure of the Saposin protein fold by a lung surfactant peptide construct of surfactant Protein B" @default.
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- W4308045202 doi "https://doi.org/10.1371/journal.pone.0276787" @default.
- W4308045202 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36327300" @default.
- W4308045202 hasPublicationYear "2022" @default.
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