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@ARTICLE{Jane:909774,
author = {Janeš, Josip Augustin and Monzel, Cornelia and Schmidt,
Daniel and Merkel, Rudolf and Seifert, Udo and Sengupta,
Kheya and Smith, Ana-Sunčana},
title = {{F}irst-{P}rinciple {C}oarse-{G}raining {F}ramework for
{S}cale-{F}ree {B}ell-{L}ike {A}ssociation and
{D}issociation {R}ates in {T}hermal and {A}ctive {S}ystems},
journal = {Physical review / X},
volume = {12},
number = {3},
issn = {2160-3308},
address = {College Park, Md.},
publisher = {APS},
reportid = {FZJ-2022-03404},
pages = {031030},
year = {2022},
abstract = {Fluctuations of surfaces that harbor reactive molecules
interacting across the intervening space strongly influence
the reaction kinetics. One such paradigmatic system is the
cell membrane, with associated proteins, binding to an
interior or an exterior scaffold—for example, the
cytoskeleton in the former and the extracellular matrix in
the latter case. Given that membrane fluctuations are
significant and regulated by the activity of the cell, we
hypothesize that these active fluctuations can be tuned to
influence ligand-receptor-mediated adhesion. However, a
comprehensive model, deriving both binding and unbinding
rates from first principles, has not yet been established,
and as such, the effect of the membrane activity on the
rates remains an open problem. Here, we solve this issue by
establishing a systematic coarse graining procedure,
providing a cascade of expressions for rates appropriate for
the observed timescale, and present a scale-free formulation
of rates. In the first step, we introduce a minimal model to
recover the so-called Bell-Dembo rates from first
principles, where the binding and unbinding rates depend on
the instantaneous position of the membrane. We then derive
the analytical coarse-grained rates for thermal
fluctuations, recovering a result that has previously been
successfully used in the literature. Finally, we expand this
framework to account for active fluctuations of the
membrane. In this step, we develop a mechanical model that
convolutes Gauss and Laplace distributed noise. This choice
may have universal features and is motivated by our analysis
of measurements in two very different cell types, namely,
human macrophages and red blood cells. We find that cell
activation enables the formation of bonds at much larger
separations between the cell and the target. This effect is
significantly greater for binding to a surface on the
extracellular compared to the intracellular side. We thus
show that active fluctuations directly influence protein
association and dissociation rates, which may have clear
physiological implications that are yet to be explored.},
cin = {IBI-2},
ddc = {530},
cid = {I:(DE-Juel1)IBI-2-20200312},
pnm = {5243 - Information Processing in Distributed Systems
(POF4-524)},
pid = {G:(DE-HGF)POF4-5243},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000859853800001},
doi = {10.1103/PhysRevX.12.031030},
url = {https://juser.fz-juelich.de/record/909774},
}