Interaction of α-Synuclein with Negatively Charged Lipid Membranes Monitored by Surface Plasmon Resonance
Katja Pirc
; National Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, Slovenia
Vesna Hodnik
; National Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, Slovenia
Nataša Poklar Ulrih
; Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, SI-1000 Ljubljana, Slovenia
Gregor Anderluh
; National Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, Slovenia
APA 6th Edition Pirc, K., Hodnik, V., Poklar Ulrih, N. i Anderluh, G. (2016). Interaction of α-Synuclein with Negatively Charged Lipid Membranes Monitored by Surface Plasmon Resonance. Croatica Chemica Acta, 89 (2), 255-260. https://doi.org/10.5562/cca2889
MLA 8th Edition Pirc, Katja, et al. "Interaction of α-Synuclein with Negatively Charged Lipid Membranes Monitored by Surface Plasmon Resonance." Croatica Chemica Acta, vol. 89, br. 2, 2016, str. 255-260. https://doi.org/10.5562/cca2889. Citirano 02.03.2021.
Chicago 17th Edition Pirc, Katja, Vesna Hodnik, Nataša Poklar Ulrih i Gregor Anderluh. "Interaction of α-Synuclein with Negatively Charged Lipid Membranes Monitored by Surface Plasmon Resonance." Croatica Chemica Acta 89, br. 2 (2016): 255-260. https://doi.org/10.5562/cca2889
Harvard Pirc, K., et al. (2016). 'Interaction of α-Synuclein with Negatively Charged Lipid Membranes Monitored by Surface Plasmon Resonance', Croatica Chemica Acta, 89(2), str. 255-260. https://doi.org/10.5562/cca2889
Vancouver Pirc K, Hodnik V, Poklar Ulrih N, Anderluh G. Interaction of α-Synuclein with Negatively Charged Lipid Membranes Monitored by Surface Plasmon Resonance. Croatica Chemica Acta [Internet]. 2016 [pristupljeno 02.03.2021.];89(2):255-260. https://doi.org/10.5562/cca2889
IEEE K. Pirc, V. Hodnik, N. Poklar Ulrih i G. Anderluh, "Interaction of α-Synuclein with Negatively Charged Lipid Membranes Monitored by Surface Plasmon Resonance", Croatica Chemica Acta, vol.89, br. 2, str. 255-260, 2016. [Online]. https://doi.org/10.5562/cca2889
Sažetak 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-sn-glycero-3-phospho-L-serine (POPS) or 1,2-dipalmitoyl-sn-glycero-3-phosphoglycerol (DPPG) and neutral 1-palmitoyl-2-oleoyl-sn-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.