Evidence map›Paper›PMID 32533943›Full record

ArticleBiophysical journal2020

Membrane Interactions of Cy3 and Cy5 Fluorophores and Their Effects on Membrane-Protein Dynamics.

Kin Lam, Emad Tajkhorshid

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.0field-weighted citation impact, top 25% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
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  5. CaThe journal of physical chemistry. B · 2025
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  9. The Transpeptidase Sortase A Binds Nucleic Acids and Mediates Mammalian Cell Labeling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Kin LamDepartment of Physics, University of Illinois at Urbana-Champaign, Urbana, Illinois; Department of Biochemistry, NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois.
Emad TajkhorshidCenter for Biophysics and Quantitative Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois; Department of Biochemistry, NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois. Electronic address: emad@life.illinois.edu.
University of Illinois Urbana-Champaign · US

Funding

WHOLE CELL SIMULATIONP41GM104601 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2012 to 2021
$19.0M
Toolkit for High-Resolution Structure and Dynamics of Functional LipidsR01GM123455 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI MORRISSEY, JAMES H., RIENSTRA, CHAD M · 2016 to 2020
$5.0M
System-Level Simulation of a Bioenergetic MembraneR01GM067887 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI TAJKHORSHID, EMAD · 2003 to 2018
$4.0M
Photochemical determination of sodium channel voltage-dependent gating and compositionR01GM122420 · NIGMS · UNIVERSITY OF IOWA · PI AHERN, CHRISTOPHER A · 2017 to 2020
$1.5M
NIGMS NIH HHS P41 GM104601NIGMS NIH HHS R01 GM067887NIGMS NIH HHS R01 GM122420NIGMS NIH HHS R01 GM123455
6 · The paper itself

Abstract

Organic fluorophores, such as Cy3 and Cy5, have been widely used as chemical labels to probe the structure and dynamics of membrane proteins. Although a number of previous studies have reported on the possibility of some of the water-soluble fluorophores to interact with lipid bilayers, detailed fluorophore-lipid interactions and, more importantly, the potential effect of such interactions on the natural dynamics of the labeled membrane proteins have not been well studied. We have performed a large set of all-atom molecular dynamics simulations employing the highly mobile membrane mimetic model to describe spontaneous partitioning of the fluorophores into lipid bilayers with different lipid compositions. Spontaneous membrane partitioning of Cy3 and Cy5 fluorophores captured in these simulations proceeds in two steps. Electrostatic interaction between the fluorophores and the lipid headgroups facilitates the initial, fast membrane association of the fluorophores, followed by slow insertion of hydrophobic moieties into the lipid bilayer core. After the conversion of the resulting membrane-bound systems to full-membrane representations, biased-exchange umbrella sampling simulations are performed for free energy calculations, revealing a higher energy barrier for partitioning into negatively charged (phosphatidylserine or phosphatidylcholine) membranes than purely zwitterionic (phosphatidylcholine or phosphatidylethanolamine) ones. Furthermore, the potential effect of fluorophore-lipid interactions on membrane proteins has been examined by covalently linking Cy5 to single- and multipass transmembrane helical proteins. Equilibrium simulations show strong position-dependent effects of Cy5-tagging on the structure and natural dynamics of membrane proteins. Interactions between the tagged protein and Cy5 were also observed. Our results suggest that fluorophore-lipid interactions can affect the structure and dynamics of membrane proteins to various extents, especially in systems with higher structural flexibility.

Indexed as

Lipid BilayersMembrane ProteinsCarbocyaninesMolecular Dynamics SimulationPhosphatidylcholinesCarbocyaninescyanine dye 5Lipid BilayersMembrane ProteinsPhosphatidylcholines

Identifiers

PMID32533943
PMCPMC7335937
OpenAlexW3033843416

What OpenQuestion holds

Textmetadata
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.