Croatica Chemica Acta, Vol. 89 No. 2, 2016.
Izvorni znanstveni članak
https://doi.org/10.5562/cca2889
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
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.
This work is licensed under a Creative Commons Attribution 4.0 International License.
Ključne riječi
surface plasmon resonance; α-synuclein; small unilamellar vesicles; lipid membranes
Hrčak ID:
170659
URI
Datum izdavanja:
21.6.2016.
Posjeta: 2.405 *