Interaction of α-Synuclein with Negatively Charged Lipid Membranes Monitored by Surface Plasmon Resonance
Aggregation of presynaptic protein α-synuclein is implicated in the development of Parkinson’s disease. Interaction of α-synuclein with lipid membranes appears to be critical for its physiological and pathological roles. Anionic lipids trigger conformational transition of α-synuclein from its native...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Croatian Chemical Society
2016-06-01
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| Series: | Croatica Chemica Acta |
| Online Access: | http://hrcak.srce.hr/file/251752 |
| _version_ | 1819274715119747072 |
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| author | Katja Pirc Vesna Hodnik Nataša Poklar Ulrih Gregor Anderluh |
| author_facet | Katja Pirc Vesna Hodnik Nataša Poklar Ulrih Gregor Anderluh |
| author_sort | Katja Pirc |
| collection | DOAJ |
| description | Aggregation of presynaptic protein α-synuclein is implicated in the development of Parkinson’s disease. Interaction of α-synuclein with lipid membranes appears to be critical for its physiological and pathological roles. Anionic lipids trigger conformational transition of α-synuclein from its natively disordered into an α-helical structure. Here we used surface plasmon resonance (SPR) to determine the affinities of α-synuclein for the small unilamellar vesicles composed of anionic 1-palmitoyl-2-oleoyl-<i>sn</i>-glycero-3-phospho-L-serine (POPS) or 1,2-dipalmitoyl-<i>sn</i>-glycero-3-phosphoglycerol (DPPG) and neutral 1-palmitoyl-2-oleoyl-<i>sn</i>-glycero-3-phosphocholine (POPC) lipids. α-Synuclein bound in a concentration dependent manner to equimolar mixtures of POPC/POPS and POPC/DPPG vesicles. The affinity of α-synuclein for POPC/POPS was ~3-fold higher than for POPC/DPPG. These results indicate that headgroup charge is not the only factor contributing to α-synuclein-membrane association.
<br><a rel="license" href="http://creativecommons.org/licenses/by/4.0/"><img alt="Creative Commons License" style="border-width:0" src="https://i.creativecommons.org/l/by/4.0/80x15.png" /></a> This work is licensed under a <a rel="license" href="http://creativecommons.org/licenses/by/4.0/">Creative Commons Attribution 4.0 International License</a>. |
| first_indexed | 2024-12-23T23:12:50Z |
| format | Article |
| id | doaj.art-e62240a7384e433abee43cd249fa09bb |
| institution | Directory Open Access Journal |
| issn | 0011-1643 1334-417X |
| language | English |
| last_indexed | 2024-12-23T23:12:50Z |
| publishDate | 2016-06-01 |
| publisher | Croatian Chemical Society |
| record_format | Article |
| series | Croatica Chemica Acta |
| spelling | doaj.art-e62240a7384e433abee43cd249fa09bb2022-12-21T17:26:37ZengCroatian Chemical SocietyCroatica Chemica Acta0011-16431334-417X2016-06-0189225526010.5562/cca2889170659Interaction of α-Synuclein with Negatively Charged Lipid Membranes Monitored by Surface Plasmon ResonanceKatja Pirc0Vesna Hodnik1Nataša Poklar Ulrih2Gregor Anderluh3National Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, SloveniaNational Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, SloveniaBiotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, SI-1000 Ljubljana, SloveniaNational Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, SloveniaAggregation of presynaptic protein α-synuclein is implicated in the development of Parkinson’s disease. Interaction of α-synuclein with lipid membranes appears to be critical for its physiological and pathological roles. Anionic lipids trigger conformational transition of α-synuclein from its natively disordered into an α-helical structure. Here we used surface plasmon resonance (SPR) to determine the affinities of α-synuclein for the small unilamellar vesicles composed of anionic 1-palmitoyl-2-oleoyl-<i>sn</i>-glycero-3-phospho-L-serine (POPS) or 1,2-dipalmitoyl-<i>sn</i>-glycero-3-phosphoglycerol (DPPG) and neutral 1-palmitoyl-2-oleoyl-<i>sn</i>-glycero-3-phosphocholine (POPC) lipids. α-Synuclein bound in a concentration dependent manner to equimolar mixtures of POPC/POPS and POPC/DPPG vesicles. The affinity of α-synuclein for POPC/POPS was ~3-fold higher than for POPC/DPPG. These results indicate that headgroup charge is not the only factor contributing to α-synuclein-membrane association. <br><a rel="license" href="http://creativecommons.org/licenses/by/4.0/"><img alt="Creative Commons License" style="border-width:0" src="https://i.creativecommons.org/l/by/4.0/80x15.png" /></a> This work is licensed under a <a rel="license" href="http://creativecommons.org/licenses/by/4.0/">Creative Commons Attribution 4.0 International License</a>.http://hrcak.srce.hr/file/251752 |
| spellingShingle | Katja Pirc Vesna Hodnik Nataša Poklar Ulrih Gregor Anderluh Interaction of α-Synuclein with Negatively Charged Lipid Membranes Monitored by Surface Plasmon Resonance Croatica Chemica Acta |
| title | Interaction of α-Synuclein with Negatively Charged Lipid Membranes Monitored by Surface Plasmon Resonance |
| title_full | Interaction of α-Synuclein with Negatively Charged Lipid Membranes Monitored by Surface Plasmon Resonance |
| title_fullStr | Interaction of α-Synuclein with Negatively Charged Lipid Membranes Monitored by Surface Plasmon Resonance |
| title_full_unstemmed | Interaction of α-Synuclein with Negatively Charged Lipid Membranes Monitored by Surface Plasmon Resonance |
| title_short | Interaction of α-Synuclein with Negatively Charged Lipid Membranes Monitored by Surface Plasmon Resonance |
| title_sort | interaction of α synuclein with negatively charged lipid membranes monitored by surface plasmon resonance |
| url | http://hrcak.srce.hr/file/251752 |
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