The Effect of a C-Terminal Peptide of Surfactant Protein B (SP-B) on Oriented Lipid Bilayers, Characterized by Solid-State 2H- and 31P-NMR
AUTOR(ES)
Yang, Tran-Chin
FONTE
The Biophysical Society
RESUMO
SP-BCTERM, a cationic, helical peptide based on the essential lung surfactant protein B (SP-B), retains a significant fraction of the function of the full-length protein. Solid-state 2H- and 31P-NMR were used to examine the effects of SP-BCTERM on mechanically oriented lipid bilayer samples. SP-BCTERM modified the multilayer structure of bilayers composed of POPC, POPG, POPC/POPG, or bovine lipid extract surfactant (BLES), even at relatively low peptide concentrations. The 31P spectra of BLES, which contains ∼1% SP-B, and POPC/POPG with 1% SP-BCTERM, look very similar, supporting a similarity in lipid interactions of SP-BCTERM and its parent protein, full-length SP-B. In the model systems, although the peptide interacted with both the oriented and unoriented fractions of the lipids, it interacted differently with the two fractions, as demonstrated by differences in lipid headgroup structure induced by the peptide. On the other hand, although SP-BCTERM induced similar disruptions in overall bilayer orientation in BLES, there was no evidence of lipid headgroup conformational changes in either the oriented or the unoriented fractions of the BLES samples. Notably, in the model lipid systems the peptide did not induce the formation of small, rapidly tumbling lipid structures, such as micelles, or of hexagonal phases, the observation of which would have provided support for functional mechanisms involving peptide-induced lipid flip-flop or stabilization of curved lipid structures, respectively.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2711426Documentos Relacionados
- Effects of pH and cholesterol on DMPA membranes: a solid state 2H- and 31P-NMR study.
- Model of interaction between a cardiotoxin and dimyristoylphosphatidic acid bilayers determined by solid-state 31P NMR spectroscopy.
- Combining solid-state and solution-state 31P NMR to study in vivo phosphorus metabolism.
- The 31P-NMR spectrum of the dodecamer d(GACGATATCGTC).
- 31P-NMR Spectroscopy of Roots of Intact Corn Seedlings 1