Fluorescence correlation spectroscopy diffusion laws in the presence of moving nanodomains

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F16%3A00457556" target="_blank" >RIV/61388955:_____/16:00457556 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.1088/0022-3727/49/11/114002" target="_blank" >http://dx.doi.org/10.1088/0022-3727/49/11/114002</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1088/0022-3727/49/11/114002" target="_blank" >10.1088/0022-3727/49/11/114002</a>

Result language

angličtina

Original language name

Fluorescence correlation spectroscopy diffusion laws in the presence of moving nanodomains

Original language description

It has been shown by means of simulations that spot variation fluorescence correlation/nspectroscopy (sv-FCS) can be used for the identification and, to some extent, also/ncharacterization of immobile lipid nanodomains in model as well as cellular plasma/nmembranes. However, in these simulations, the nanodomains were assumed to be stationary,/nwhereas they actually tend to move like the surrounding lipids. In the present study, we/ninvestigated how such domain movement influences the diffusion time/spot-size dependence/nobserved in FCS experiments, usually referred to as diffusion law’ analysis. We show/nthat domain movement might mask the effects of the anomalous’ diffusion characteristics/nof membrane lipids or proteins predicted for stationary domains, making it difficult to/nidentify such moving nanodomains by sv-FCS. More specifically, our simulations indicate/nthat (i) for domains moving up to a factor of 2.25 slower than the surrounding lipids, such/nimpeded diffusion cannot be observed and the diffusion behaviour of the proteins or lipids is/nindistinguishable from that of freely diffusing molecules, i.e. nanodomains are not detected;/n(ii) impeded protein/lipid diffusion behaviour can be observed in experiments where the radii/nof the detection volume are similar in size to the domain radii, the domain diffusion is about/n10 times slower than that of the lipids, and the probes show a high affinity to the domains;/nand (iii) presence of nanodomains can only be reliably detected by diffraction limited sv-FCS/nwhen the domains move very slowly (about 200 times slower than the lipid diffusion). As/nnanodomains are expected to be in the range of tens of nanometres and most probes show/nlow affinities to such domains, sv-FCS is limited to stationary domains and/or STED-FCS./nHowever, even for that latter technique, diffusing domains smaller than 50 nm in radius are/nhardly detectable by FCS diffusion time/spot-size dependencies.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CF - Physical chemistry and theoretical chemistry

OECD FORD branch

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Project

<a href="/en/project/GC14-03141J" target="_blank" >GC14-03141J: Exploring the structure function relationship of membrane-pore-forming FGF2 oligomers - a single molecule approach</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2016

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Physics D-Applied Physics

ISSN

0022-3727

e-ISSN

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Volume of the periodical

49

Issue of the periodical within the volume

11

Country of publishing house

GB - UNITED KINGDOM

Number of pages

11

Pages from-to

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UT code for WoS article

000371007100003

EID of the result in the Scopus database

2-s2.0-84960096929