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 |
| Published: |
Croatian Chemical Society
2016-06-01
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| Series: | Croatica Chemica Acta |
| Online Access: | http://hrcak.srce.hr/file/251752 |
| Summary: | 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>. |
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| ISSN: | 0011-1643 1334-417X |