Solid-state NMR and simulation studies of equinatoxin II N-terminus interaction with lipid bilayers.
The interaction with model membranes of a peptide, EqtII(1-32), corresponding to the N-terminal region of the pore-forming toxin equinatoxin II (EqtII) has been studied using solid-state NMR and molecular dynamics (MD) simulations. The distances between specifically labeled nuclei in [(19)F-para]Phe...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
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2010
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| _version_ | 1797100791000989696 |
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| author | Lam, Y Hung, A Norton, R Separovic, F Watts, A |
| author_facet | Lam, Y Hung, A Norton, R Separovic, F Watts, A |
| author_sort | Lam, Y |
| collection | OXFORD |
| description | The interaction with model membranes of a peptide, EqtII(1-32), corresponding to the N-terminal region of the pore-forming toxin equinatoxin II (EqtII) has been studied using solid-state NMR and molecular dynamics (MD) simulations. The distances between specifically labeled nuclei in [(19)F-para]Phe16-[1-(13)C]Leu19 and [(19)F-para]Phe16-[(15)N]Leu23 analogs of EqtII(1-32) measured by REDOR in lyophilized peptide were in agreement with published crystal and solution structures. However, in both DMPC and mixed DMPC:SM membrane environments, significant changes in the distances between the labeled amino acid pairs were observed, suggesting changes in helical content around the experimentally studied region, 16-23, in the presence of bilayers. (19)F-(31)P REDOR experiments indicated that the aromatic ring of Phe16 is in contact with lipid headgroups in both membrane environments. For the DMPC:SM mixed bilayers, a closer interaction between Phe16 side chains and lipid headgroups was observed, but an increase in distances was observed for both labeled amino acid pairs compared with those measured for EqtII(1-32) in pure DMPC bilayers. The observed differences between DMPC and DMPC:SM bilayers may be due to the greater affinity of EqtII for the latter. MD simulations of EqtII(1-32) in water, on a pure DMPC bilayer, and on a mixed DMPC:SM bilayer indicate significant peptide secondary structural differences in the different environments, with the DMPC-bound peptide adopting helical formations at residues 16-24, whereas the DMPC:SM-bound peptide exhibits a longer helical stretch, which may contribute to its enhanced activity against PC:SM compared with pure PC bilayers. Proteins 2010. (c) 2009 Wiley-Liss, Inc. |
| first_indexed | 2024-03-07T05:42:37Z |
| format | Journal article |
| id | oxford-uuid:e6184bfd-f36b-4108-a6fb-e8b92ad28d71 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T05:42:37Z |
| publishDate | 2010 |
| record_format | dspace |
| spelling | oxford-uuid:e6184bfd-f36b-4108-a6fb-e8b92ad28d712022-03-27T10:28:50ZSolid-state NMR and simulation studies of equinatoxin II N-terminus interaction with lipid bilayers.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:e6184bfd-f36b-4108-a6fb-e8b92ad28d71EnglishSymplectic Elements at Oxford2010Lam, YHung, ANorton, RSeparovic, FWatts, AThe interaction with model membranes of a peptide, EqtII(1-32), corresponding to the N-terminal region of the pore-forming toxin equinatoxin II (EqtII) has been studied using solid-state NMR and molecular dynamics (MD) simulations. The distances between specifically labeled nuclei in [(19)F-para]Phe16-[1-(13)C]Leu19 and [(19)F-para]Phe16-[(15)N]Leu23 analogs of EqtII(1-32) measured by REDOR in lyophilized peptide were in agreement with published crystal and solution structures. However, in both DMPC and mixed DMPC:SM membrane environments, significant changes in the distances between the labeled amino acid pairs were observed, suggesting changes in helical content around the experimentally studied region, 16-23, in the presence of bilayers. (19)F-(31)P REDOR experiments indicated that the aromatic ring of Phe16 is in contact with lipid headgroups in both membrane environments. For the DMPC:SM mixed bilayers, a closer interaction between Phe16 side chains and lipid headgroups was observed, but an increase in distances was observed for both labeled amino acid pairs compared with those measured for EqtII(1-32) in pure DMPC bilayers. The observed differences between DMPC and DMPC:SM bilayers may be due to the greater affinity of EqtII for the latter. MD simulations of EqtII(1-32) in water, on a pure DMPC bilayer, and on a mixed DMPC:SM bilayer indicate significant peptide secondary structural differences in the different environments, with the DMPC-bound peptide adopting helical formations at residues 16-24, whereas the DMPC:SM-bound peptide exhibits a longer helical stretch, which may contribute to its enhanced activity against PC:SM compared with pure PC bilayers. Proteins 2010. (c) 2009 Wiley-Liss, Inc. |
| spellingShingle | Lam, Y Hung, A Norton, R Separovic, F Watts, A Solid-state NMR and simulation studies of equinatoxin II N-terminus interaction with lipid bilayers. |
| title | Solid-state NMR and simulation studies of equinatoxin II N-terminus interaction with lipid bilayers. |
| title_full | Solid-state NMR and simulation studies of equinatoxin II N-terminus interaction with lipid bilayers. |
| title_fullStr | Solid-state NMR and simulation studies of equinatoxin II N-terminus interaction with lipid bilayers. |
| title_full_unstemmed | Solid-state NMR and simulation studies of equinatoxin II N-terminus interaction with lipid bilayers. |
| title_short | Solid-state NMR and simulation studies of equinatoxin II N-terminus interaction with lipid bilayers. |
| title_sort | solid state nmr and simulation studies of equinatoxin ii n terminus interaction with lipid bilayers |
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