ArticleBiophysical journal2007
Investigating the interaction of saposin C with POPS and POPC phospholipids: a solid-state NMR spectroscopic study.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 22 citations in OpenAlex.
- Design of Novel Saposin-like Bacteriocins Using a Hybrid Approach.Probiotics and antimicrobial proteins · 2025Article
- The Influence of Short Motifs on the Anticancer Activity of HB43 Peptide.Pharmaceutics · 2022Article
- Insights into the mechanism of membrane fusion induced by the plant defense element, plant-specific insert.The Journal of biological chemistry · 2020Article
- Simulation of lipid bilayer self-assembly using all-atom lipid force fields.Physical chemistry chemical physics : PCCP · 2016Article
- Solid-state NMR (31)P paramagnetic relaxation enhancement membrane protein immersion depth measurements.The journal of physical chemistry. B · 2014Article
- Reinforcing the membrane-mediated mechanism of action of the anti-tuberculosis candidate drug thioridazine with molecular simulations.Journal of computer-aided molecular design · 2014Article
- Penetration depth of surfactant peptide KL4 into membranes is determined by fatty acid saturation.Biophysical journal · 2009Article
- Interactions of the C-terminus of lung surfactant protein B with lipid bilayers are modulated by acyl chain saturation.Biochimica et biophysica acta · 2008Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The interaction of Saposin C (Sap C) with negatively charged phospholipids such as phosphatidylserine (PS) is essential for its biological function. In this study, Sap C (initially protonated in a weak acid) was inserted into multilamellar vesicles (MLVs) consisting of either 1-palmitoyl-2-oleoyl-sn-glycero-3-[phospho-L-serine] (negatively charged, POPS) or 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (neutrally charged, POPC). The MLVs were then investigated using solid-state NMR spectroscopy under neutral pH (7.0) conditions. The (2)H and (31)P solid-state NMR spectroscopic data of Sap C-POPS and Sap C-POPC MLVs (prepared under the same conditions) were compared using the (2)H order parameter profiles of the POPC-d(31) or POPS-d(31) acyl chains as well as the (31)P chemical shift anisotropy width and (31)P T(1) relaxation times of the phospholipids headgroups. All those solid-state NMR spectroscopic approaches indicate that protonated Sap C disturbs the POPS bilayers and not the POPC lipid bilayers. These observations suggest for the first time that protonated Sap C inserts into PS bilayers and forms a stable complex with the lipids even after resuspension under neutral buffer conditions. Additionally, (31)P solid-state NMR spectroscopic studies of mechanically oriented phospholipids on glass plates were conducted and perturbation effect of Sap C on both POPS and POPC bilayers was compared. Unlike POPC bilayers, the data indicates that protonated Sap C (initially protonated in a weak acid) was unable to produce well-oriented POPS bilayers on glass plates at neutral pH. Conversely, unprotonated Sap C (initially dissolved in a neutral buffer) did not interact significantly with POPS phospholipids allowing them to produce well-oriented bilayers at neutral pH.
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