Abstract
| Original language | Undefined |
|---|---|
| Pages (from-to) | 2257-2262 |
| Journal | Small |
| Volume | 11 |
| Issue number | 19 |
| DOIs | |
| Publication status | Published - 15 Jan 2015 |
Keywords
- IR-95651
- METIS-309191
Cite this
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Alpha-Synuclein Amyloid Oligomers Act as Multivalent Nanoparticles to Cause Hemifusion in Negatively Charged Vesicles. / Stefanovic, A.; Claessens, Mireille Maria Anna Elisabeth; Blum, Christian; Subramaniam, Vinod.
In: Small, Vol. 11, No. 19, 15.01.2015, p. 2257-2262.Research output: Contribution to journal › Article › Academic › peer-review
TY - JOUR
T1 - Alpha-Synuclein Amyloid Oligomers Act as Multivalent Nanoparticles to Cause Hemifusion in Negatively Charged Vesicles
AU - Stefanovic, A.
AU - Claessens, Mireille Maria Anna Elisabeth
AU - Blum, Christian
AU - Subramaniam, Vinod
PY - 2015/1/15
Y1 - 2015/1/15
N2 - Multivalent membrane binding sites on the α-synuclein oligomer result in clustering of vesicles and hemifusion of negatively charged model membranes. These multivalent, biological nanoparticles are reminiscent of inorganic nanoparticles in their interactions with membranes. Alpha-synuclein oligomers induce lipid exchange efficiently, with fewer than 10 oligomers/vesicle required to complete hemifusion. No full fusion or vesicle content mixing is observed
AB - Multivalent membrane binding sites on the α-synuclein oligomer result in clustering of vesicles and hemifusion of negatively charged model membranes. These multivalent, biological nanoparticles are reminiscent of inorganic nanoparticles in their interactions with membranes. Alpha-synuclein oligomers induce lipid exchange efficiently, with fewer than 10 oligomers/vesicle required to complete hemifusion. No full fusion or vesicle content mixing is observed
KW - IR-95651
KW - METIS-309191
U2 - 10.1002/smll.201402674
DO - 10.1002/smll.201402674
M3 - Article
VL - 11
SP - 2257
EP - 2262
JO - Small
JF - Small
SN - 1613-6810
IS - 19
ER -