Quantification of protein–lipid selectivity using FRET

Loura, Luís M. S.; Prieto, Manuel; Fernandes, Fábio

doi:10.1007/s00249-009-0532-z

Cited by 39 publications

(30 citation statements)

References 69 publications

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“…However, this kind of formalisms has been characterized by either severe simplifying approximations (Gutierrez-Merino, 1981; Brown et al, 2007a,b) or relying to some extent to numerical results (Towles et al, 2007; see Loura et al, 2010a for a detailed discussion), precluding their widespread use.…”

Section: Numerical and Simplified Analytical Treatments Of Fret In Nomentioning

confidence: 99%

FRET in membrane biophysics: an overview

Loura

Prieto²

2011

Front. Physio.

106

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Förster resonance energy transfer (FRET), in most applications used as a “spectroscopic ruler,” allows an easy determination of the donor-acceptor intermolecular distance. However, the situation becomes complex in membranes, since around each donor there is an ensemble of acceptors at non-correlated distances. In this review, state-of-the-art methodologies for this situation are presented, usually involving time-resolved data and model fitting. This powerful approach can be used to study the occurrence of phase separation (“rafts” or other type of domains), allowing their detection as well as size evaluation. Formalisms for studying lipid–protein and protein–protein interactions according to specific topologies are also addressed. The advantages and added complexity of a specific type of FRET (energy homotransfer or energy migration) are described, as well as applications of FRET under the microscope.

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Section: Numerical and Simplified Analytical Treatments Of Fret In Nomentioning

confidence: 99%

FRET in membrane biophysics: an overview

Loura

Prieto²

2011

Front. Physio.

106

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show abstract

“…In this case FRET (or quenching) is measured from a peptide-attached fluorophore to a labeled lipid [162]. Preferential interaction with that particular lipid will be demonstrated by a quenching efficiency higher than that expected for a random distribution of acceptors in the plane of the membrane.…”

Section: Lateral Mobility and Domain Formationmentioning

confidence: 99%

Fluorescence spectroscopy and molecular dynamics simulations in studies on the mechanism of membrane destabilization by antimicrobial peptides

Bocchinfuso

Bobone

Meisina

et al. 2011

Cell. Mol. Life Sci.

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Since their initial discovery, 30 years ago, antimicrobial peptides (AMPs) have been intensely investigated as a possible solution to the increasing problem of drug-resistant bacteria. The interaction of antimicrobial peptides with the cellular membrane of bacteria is the key step of their mechanism of action. Fluorescence spectroscopy can provide several structural details on peptide-membrane systems, such as partition free energy, aggregation state, peptide position and orientation in the bilayer, and the effects of the peptides on the membrane order. However, these "low-resolution" structural data are hardly sufficient to define the structural requirements for the pore formation process. Molecular dynamics simulations, on the other hand, provide atomic-level information on the structure and dynamics of the peptide-membrane system, but they need to be validated experimentally. In this review we summarize the information that can be obtained by both approaches, highlighting their versatility and complementarity, suggesting that their synergistic application could lead to a new level of insight into the mechanism of membrane destabilization by AMPs.

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“…Variations in the separation and spatial arrangement of chromophores lead to alterations in FRET, that can be monitored under steady-state and/or time-resolved conditions. On a very basic level, FRET may be employed as a phenomenological indicator of molecular proximity, and a large body of work has been reported describing such qualitative applications [30]. However, to take full advantage of the technique's potential, models that describe the dependence of FRET observables on the structural properties of the system under study are required.…”

Section: The Biological Importance Of Electrostatic Lipid-protein Intmentioning

confidence: 99%

Electrostatically driven lipid–protein interaction: Answers from FRET

Fernandes

Coutinho

Prieto

et al. 2015

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Electrostatics govern the association of a large number of proteins with cellular membranes. In some cases, these proteins present specialized lipid-binding modules or membrane targeting domains while in other cases association is achieved through nonspecific interaction of unstructured clusters of basic residues with negatively charged lipids. Given its spatial resolution in the nanometer range, Förster resonance energy transfer (FRET) is a powerful tool to give insight into protein-lipid interactions and provide molecular level information which is difficult to retrieve with other spectroscopic techniques. In this review we present and discuss the basic formalisms of both hetero- and homo-FRET pertinent to the most commonly encountered problems in lipid-protein interaction studies and highlight some examples of implementations of different FRET methodologies to characterize lipid/protein systems in which electrostatic interactions play a crucial role. This article is part of a Special Issue entitled: Lipid-protein interactions.

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Quantification of protein–lipid selectivity using FRET

Cited by 39 publications

References 69 publications

FRET in membrane biophysics: an overview

FRET in membrane biophysics: an overview

Fluorescence spectroscopy and molecular dynamics simulations in studies on the mechanism of membrane destabilization by antimicrobial peptides

Electrostatically driven lipid–protein interaction: Answers from FRET

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