A Kakio

A Onufriev

Artur Matysik

B Hess

B Windschiegl

BC Yowler

CA Lasagna-Reeves

CM Yip

D Lingwood

D Van der Spoel

D Zhang

DA Bateman

E Lindahl

G Bussi

GM Kuziemko

H Ewers

HJC Berendsen

J Fantini

J McLaurin

J Sankaran

JJ Kremer

JV Rocheleau

K Bacia

K Ikeda

K Yanagisawa

Kamila Oglęcka

L Johannes

L Saavedra

LP Choo-Smith

M Levy

M Stefl

M Wakabayashi

Manoj Manna

Maria Ruhnow

Michael Koval

MJ Widenbrant

MP Williamson

MR Baldwin

N Yamamoto

P Antes

P Critchley

R Pellizzari

R Roy

Rachel Kraut

RD Johnson

RH Swendsen

S Hebbar

S Inaba

S Manes

S Nag

S Steinert

SA Poulsen

SA Waschuk

Susana Geifman-Shochat

T Ariga

T Dertinger

T Valdes-Gonzalez

Thorsten Wohland

Tim Lauterbach

TS van Zanten

V Hornak

W Kabsch

W Romer

WI Weis

Yaofeng Wang

YC Lee

Yudi Wisantoso

Yuguang Mu

Z Petrasek

PubMed

Organized assembly or aggregation of sphingolipid-binding ligands, such as certain toxins and pathogens, has been suggested to increase binding affinity of the ligand to the cell membrane and cause membrane reorganization or distortion. Here we show that the diffusion behavior of the fluorescently tagged sphingolipid-interacting peptide probe SBD (Sphingolipid Binding Domain) is altered by modifications in the construction of the peptide sequence that both result in a reduction in binding to ganglioside-containing supported lipid membranes, and at the same time increase aggregation on the cell plasma membrane, but that do not change relative amounts of secondary structural features. We tested the effects of modifying the overall charge and construction of the SBD probe on its binding and diffusion behavior, by Surface Plasmon Resonance (SPR; Biacore) analysis on lipid surfaces, and by Fluorescence Correlation Spectroscopy (FCS) on live cells, respectively. SBD binds preferentially to membranes containing the highly sialylated gangliosides GT1b and GD1a. However, simple charge interactions of the peptide with the negative ganglioside do not appear to be a critical determinant of binding. Rather, an aggregation-suppressing amino acid composition and linker between the fluorophore and the peptide are required for optimum binding of the SBD to ganglioside-containing supported lipid bilayer surfaces, as well as for interaction with the membrane. Interestingly, the strength of interactions with ganglioside-containing artificial membranes is mirrored in the diffusion behavior by FCS on cell membranes, with stronger binders displaying similar characteristic diffusion profiles. Our findings indicate that for aggregation-prone peptides, aggregation occurs upon contact with the cell membrane, and rather than giving a stronger interaction with the membrane, aggregation is accompanied by weaker binding and complex diffusion profiles indicative of heterogeneous diffusion behavior in the probe population.Published versio

Wohland, Thorsten

Kraut, Rachel

Geifman-Shochat, Susana

Lauterbach, Tim

Manna, Manoj

Ruhnow, Maria

Wisantoso, Yudi

Wang, Yaofeng

Matysik, Artur

Oglęcka, Kamila

Mu, Yuguang

Digital Repository - Nanyang Technological University

PLoS ONE

Weak glycolipid binding of a microdomain-tracer peptide correlates with aggregation and slow diffusion on cell membranes

<div><p>Organized assembly or aggregation of sphingolipid-binding ligands, such as certain toxins and pathogens, has been suggested to increase binding affinity of the ligand to the cell membrane and cause membrane reorganization or distortion. Here we show that the diffusion behavior of the fluorescently tagged sphingolipid-interacting peptide probe SBD (Sphingolipid Binding Domain) is altered by modifications in the construction of the peptide sequence that both result in a reduction in binding to ganglioside-containing supported lipid membranes, and at the same time increase aggregation on the cell plasma membrane, but that do not change relative amounts of secondary structural features. We tested the effects of modifying the overall charge and construction of the SBD probe on its binding and diffusion behavior, by Surface Plasmon Resonance (SPR; Biacore) analysis on lipid surfaces, and by Fluorescence Correlation Spectroscopy (FCS) on live cells, respectively. SBD binds preferentially to membranes containing the highly sialylated gangliosides GT1b and GD1a. However, simple charge interactions of the peptide with the negative ganglioside do not appear to be a critical determinant of binding. Rather, an aggregation-suppressing amino acid composition and linker between the fluorophore and the peptide are required for optimum binding of the SBD to ganglioside-containing supported lipid bilayer surfaces, as well as for interaction with the membrane. Interestingly, the strength of interactions with ganglioside-containing artificial membranes is mirrored in the diffusion behavior by FCS on cell membranes, with stronger binders displaying similar characteristic diffusion profiles. Our findings indicate that for aggregation-prone peptides, aggregation occurs upon contact with the cell membrane, and rather than giving a stronger interaction with the membrane, aggregation is accompanied by weaker binding and complex diffusion profiles indicative of heterogeneous diffusion behavior in the probe population.</p> </div

Tim Lauterbach (112062)

Manoj Manna (112068)

Maria Ruhnow (112071)

Yudi Wisantoso (112073)

Yaofeng Wang (112076)

Artur Matysik (112078)

Kamila Oglęcka (112081)

Yuguang Mu (29465)

Susana Geifman-Shochat (112085)

Thorsten Wohland (112087)

Rachel Kraut (58808)

The Francis Crick Institute

Weak Glycolipid Binding of a Microdomain-Tracer Peptide Correlates with Aggregation and Slow Diffusion on Cell Membranes

Lauterbach Tim

Manna Manoj

Ruhnow Maria

Wisantoso Yudi

Wang Yaofeng

Matysik Artur

Oglęcka Kamila

Mu Yuguang

Geifman-Shochat Susana

Wohland Thorsten

Kraut Rachel

Public Library of Science (PLOS)

Crossref

Organized assembly or aggregation of sphingolipid-binding ligands, such as certain toxins and pathogens, has been suggested to increase binding affinity of the ligand to the cell membrane and cause membrane reorganization or distortion. Here we show that the diffusion behavior of the fluorescently tagged sphingolipid-interacting peptide probe SBD (Sphingolipid Binding Domain) is altered by modifications in the construction of the peptide sequence that both result in a reduction in binding to ganglioside-containing supported lipid membranes, and at the same time increase aggregation on the cell plasma membrane, but that do not change relative amounts of secondary structural features. We tested the effects of modifying the overall charge and construction of the SBD probe on its binding and diffusion behavior, by Surface Plasmon Resonance (SPR; Biacore) analysis on lipid surfaces, and by Fluorescence Correlation Spectroscopy (FCS) on live cells, respectively. SBD binds preferentially to membranes containing the highly sialylated gangliosides GT1b and GD1a. However, simple charge interactions of the peptide with the negative ganglioside do not appear to be a critical determinant of binding. Rather, an aggregation-suppressing amino acid composition and linker between the fluorophore and the peptide are required for optimum binding of the SBD to ganglioside-containing supported lipid bilayer surfaces, as well as for interaction with the membrane. Interestingly, the strength of interactions with ganglioside-containing artificial membranes is mirrored in the diffusion behavior by FCS on cell membranes, with stronger binders displaying similar characteristic diffusion profiles. Our findings indicate that for aggregation-prone peptides, aggregation occurs upon contact with the cell membrane, and rather than giving a stronger interaction with the membrane, aggregation is accompanied by weaker binding and complex diffusion profiles indicative of heterogeneous diffusion behavior in the probe population

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https://figshare.com/articles/Weak_Glycolipid_Binding_of_a_Microdomain_Tracer_Peptide_Correlates_with_Aggregation_and_Slow_Diffusion_on_Cell_Membranes__/116080

Weak Glycolipid Binding of a Microdomain-Tracer Peptide Correlates with Aggregation and Slow Diffusion on Cell Membranes

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Digital Repository - Nanyang Technological University

The Francis Crick Institute

Public Library of Science (PLOS)

Crossref

Directory of Open Access Journals