Electrostatically driven lipid–protein interaction: Answers from FRET

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

doi:10.1016/j.bbamem.2015.02.023

Cited by 14 publications

(5 citation statements)

References 89 publications

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“…CuPc molecules in the hybrid membranes served as acceptors. Based on FRET theory, as the distance between the donor and the acceptor becomes lesser, then the energy transfer between the two molecules becomes more effective. − Therefore, it is possible to estimate the location of CuPc molecules in hybrid membranes based on energy transfer efficiency measurements.…”

Section: Resultsmentioning

confidence: 99%

Formation and Characterization of Air-Stable Lipid Bilayer Membranes Incorporated with Phthalocyanine Molecules

Feng

Yamaura

et al. 2019

J. Phys. Chem. B

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Bilayer lipid membranes (BLMs) are used as basic frameworks for biosensors and biohybrid devices due to their unique properties, which include ultrathin thickness, ultrahigh resistivity, and self-assembling ability. However, BLMs can only form and maintain their structure in aqueous environments, which pose significant limitations to their use. In this work, we report on the formation of highly uniform hybrid BLMs at a water/air interface through self-assembly by simply doping the BLMs with a functional organic molecule, copper(II) 2,9,16,23-tetra-tert-butyl-29H,31H-phthalocyanine (CuPc). By transferring the membrane onto substrates, we were able to produce stable hybrid BLMs under anhydrous conditions. Atomic force microscopy and X-ray diffraction measurements confirmed that the hybrid membranes were composed of single, highly uniform BLMs or stacks of BLMs. Fluorescence resonance energy transfer measurements indicated that the CuPc molecules were located between the hydrophobic tails of lipid molecules, forming a sandwich structure in the hybrid membranes. The hybrid BLMs fabricated by this method substantially expand the range of applications of BLMs to solid-state devices.

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Section: Resultsmentioning

confidence: 99%

Formation and Characterization of Air-Stable Lipid Bilayer Membranes Incorporated with Phthalocyanine Molecules

Feng

Yamaura

et al. 2019

J. Phys. Chem. B

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“… a References cited in this table: , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , . …”

Section: Pi-plc Membrane Binding and Interactions With Phospholipidsunclassified

Search and Subvert: Minimalist Bacterial Phosphatidylinositol-Specific Phospholipase C Enzymes

Roberts

Goldstein

et al. 2018

Chem. Rev.

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Phosphatidylinositol-specific phospholipase C (PI-PLC) enzymes from Gram-positive bacteria are secreted virulence factors that aid in downregulating host immunity. These PI-PLCs are minimalist peripheral membrane enzymes with a distorted (βα) TIM barrel fold offering a conserved and stable scaffold for the conserved catalytic amino acids while membrane recognition is achieved mostly through variable loops. Decades of experimental and computational research on these enzymes have revealed the subtle interplay between molecular mechanisms of catalysis and membrane binding, leading to a semiquantitative model for how they find, bind, and cleave their respective substrates on host cell membranes. Variations in sequence and structure of their membrane binding sites may correlate with how enzymes from different Gram-positive bacteria search for their particular targets on the membrane. Detailed molecular characterization of protein-lipid interactions have been aided by cutting-edge methods ranging from P field-cycling NMR relaxometry to monitor protein-induced changes in phospholipid dynamics to molecular dynamics simulations to elucidate the roles of electrostatic and cation-π interactions in lipid binding to single molecule fluorescence measurements of dynamic interactions between PI-PLCs and vesicles. This toolkit is readily applicable to other peripheral membrane proteins including orthologues in Gram-negative bacteria and more recently discovered eukaryotic minimalist PI-PLCs.

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“…4 There are two primary ways that lipids affect protein structure and function. The first is that protein function is influenced by specific protein-lipid interactions that depend on the individual chemical and structural characteristics of the lipids [5][6][7] , e.g. head group, alkyl chain length and degree of unsaturation.…”

Section: Introductionmentioning

confidence: 99%

“…There are two primary ways that lipids affect protein structure and function. The first is that protein function is influenced by specific protein–lipid interactions that depend on the individual chemical and structural characteristics of the lipids, − for example, head group, alkyl chain length, and degree of unsaturation. The second is that protein function is influenced by self-association properties that result from collective properties, − for example, fluidity, shape, and packing properties.…”

Section: Introductionmentioning

confidence: 99%

Role of Lipid Composition on the Interaction between a Tryptophan-Rich Protein and Model Bacterial Membranes

et al. 2016

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The interaction between tryptophan-rich puroindoline proteins and model bacterial membranes at the air-liquid interface has been investigated by FTIR spectroscopy, surface pressure measurements, and Brewster angle microscopy. The role of different lipid constituents on the interactions between lipid membrane and protein was studied using wild type (Pin-b) and mutant (Trp44 to Arg44 mutant, Pin-bs) puroindoline proteins. The results show differences in the lipid selectivity of the two proteins in terms of preferential binding to specific lipid head groups in mixed lipid systems. Pin-b wild type was able to penetrate mixed layers of phosphatidylethanolamine (PE) and phosphatidylglycerol (PG) head groups more deeply compared to the mutant Pin-bs. Increasing saturation of the lipid tails increased penetration and adsorption of Pin-b wild type, but again the response of the mutant form differed. The results provide insight as to the role of membrane architecture, lipid composition, and fluidity on antimicrobial activity of proteins. Data show distinct differences in the lipid binding behavior of Pin-b as a result of a single residue mutation, highlighting the importance of hydrophobic and charged amino acids in antimicrobial protein and peptide activity.

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Electrostatically driven lipid–protein interaction: Answers from FRET

Cited by 14 publications

References 89 publications

Formation and Characterization of Air-Stable Lipid Bilayer Membranes Incorporated with Phthalocyanine Molecules

Formation and Characterization of Air-Stable Lipid Bilayer Membranes Incorporated with Phthalocyanine Molecules

Search and Subvert: Minimalist Bacterial Phosphatidylinositol-Specific Phospholipase C Enzymes

Role of Lipid Composition on the Interaction between a Tryptophan-Rich Protein and Model Bacterial Membranes

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