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@ARTICLE{Yu:844894,
author = {Yu, Qingfen and Othman, Sameh and Dasgupta, Sabyasachi and
Auth, Thorsten and Gompper, Gerhard},
title = {{N}anoparticle wrapping at small non-spherical vesicles:
curvatures at play},
journal = {Nanoscale},
volume = {10},
number = {14},
issn = {2040-3372},
address = {Cambridge},
publisher = {RSC Publ.},
reportid = {FZJ-2018-02236},
pages = {6445 - 6458},
year = {2018},
abstract = {Nanoparticles in biological systems encounter lipid-bilayer
membranes as barriers. They interact with plasma membranes,
membranous organelles, such as the endoplasmic reticulum and
the Golgi apparatus, the nucleus, and intracellular and
extracellular vesicles, such as autophagosomes, lysosomes,
and exosomes. Extracellular vesicles have recently attracted
particular attention, as they are involved in the
transmission of biological signals and as regulators for
biological processes. For example, exosomes, small vesicles
containing proteins, mRNA, and miRNA, that are released by
cells into the extracellular environment, have been
suggested to participate in tumor metastasis. Furthermore,
vesicles can be applied as targeted-drug-delivery systems.
We systematically characterize wrapping of spherical
nanoparticles that enter and exit vesicles, depending on
particle size, vesicle size, vesicle reduced volume, and
membrane spontaneous curvature. We predict the complex
wrapping behavior, in particular for large
particle-to-vesicle size ratios, where the shape changes of
the free membrane contribute significantly to the
deformation energy and where nanoparticle wrapping
transitions and vesicle shape transitions are coupled.
Partial-wrapped membrane-bound particles impose boundary
conditions on the membrane that stabilise oblates and
stomatocytes for particle entry, and prolates and
stomatocytes for particle exit. Our results suggest that
nanoparticles may stimulate autophagocytic engulfment, which
would facilitate transport of the nanoparticles into
lysosomes and would lead to subsequent degradation of
nanoparticle-attached proteins.},
cin = {ICS-2},
ddc = {600},
cid = {I:(DE-Juel1)ICS-2-20110106},
pnm = {552 - Engineering Cell Function (POF3-552)},
pid = {G:(DE-HGF)POF3-552},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:29565057},
UT = {WOS:000429530400025},
doi = {10.1039/C7NR08856F},
url = {https://juser.fz-juelich.de/record/844894},
}