Insertion and activation of functional Bacteriorhodopsin in a floating bilayer

Mukhina, Tetiana; Gerelli, Yuri; Hemmerle, Arnaud; Koutsioubas, Alexandros; Kovalev, Kirill; Teulon, Jean‐Marie; Pellequer, Jean‐Luc; Daillant, Jean; Charitat, Thierry; Fragneto, Giovanna

doi:10.1016/j.jcis.2021.03.155

Cited by 4 publications

(3 citation statements)

References 67 publications

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“…In particular, aided by the possibility to vary the scattering length density (SLD) contrast , between the substrate, the adsorbed film, and the background buffer by exchanging protium ( 1 H) with deuterium ( 2 H), NR has been shown to offer absolute thickness determinations with sub-nanometer precision of biomolecular films and their internal structure, even for multilayered systems . In the case of SLBs, NR was not only successfully used to quantify minute differences in the thickness of hydrophobic and hydrophilic portions of SLBs made from different lipid compositions but also structural alterations induced by changes in environmental conditions , and biomolecular interactions . However, while thickness determination is relatively straightforward, separation distance determination is particularly challenging using NR, as NR requires strong SLD contrasts in the direction orthogonal to the interface and a well-defined layered structure, so far only realized for homogeneous flat layers. ,, Thus, due to the geometry of spherically shaped nanoparticles, NR has been rarely used for in-depth characterization of adsorbed nanoparticles.…”

Section: Introductionmentioning

confidence: 99%

Probing the Separation Distance between Biological Nanoparticles and Cell Membrane Mimics Using Neutron Reflectometry with Sub-Nanometer Accuracy

et al. 2022

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Nanoparticle interactions with cellular membranes are controlled by molecular recognition reactions and regulate a multitude of biological processes, including virus infections, biological nanoparticle-mediated cellular communication, and drug delivery applications. Aided by the design of various supported cell membrane mimics, multiple methods have been employed to investigate these types of interactions, revealing information on nanoparticle coverage, interaction kinetics, as well as binding strength; however, precise quantification of the separation distance across which these delicate interactions occur remains elusive. Here, we demonstrate that carefully designed neutron reflectometry (NR) experiments followed by an attentive selection and application of suitable theoretical models offer a means to quantify the distance separating biological nanoparticles from a supported lipid bilayer (SLB) with sub-nanometer precision. The distance between the nanoparticles and SLBs was tuned by exploiting either direct adsorption or specific binding using DNA tethers with different conformations, revealing separation distances of around 1, 3, and 7 nm with nanometric accuracy. We also show that NR provides precise information on nanoparticle coverage, size distribution, material composition, and potential structural changes in the underlying planar SLB induced upon nanoparticle binding. The precision with which these parameters could be quantified should pave an attractive path for investigations of the interactions between nanoparticles and interfaces at length scales and resolutions that were previously inaccessible. This thus makes it possible to, for example, gain an in-depth understanding of the molecular recognition reactions of inorganic and biological nanoparticles with cellular membranes.

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Section: Introductionmentioning

confidence: 99%

Probing the Separation Distance between Biological Nanoparticles and Cell Membrane Mimics Using Neutron Reflectometry with Sub-Nanometer Accuracy

et al. 2022

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“…L-weight filter has been proved as a powerful processing tool for AFM molecular images for the studies of estimation of molecular size of an anonymized protein 29 to DNA-HU protein binding reaction, 31 and from fibrillation of cytosolic abundant heat-soluble proteins from tardigrades 32 to the deposition of bacteriorhodopsin with lipid membranes on mica. 33 It has a similar function as the well-known Laplacian mask 34 to sharpen the boundary of the image object, and substantially diminishes severe broadening effects brought by the AFM probing tip. It has also been implicitly implemented in the DeStripe program for removing stripping noise.…”

Section: Methodology 1| Afm Imaging and L-weight Filtermentioning

confidence: 99%

Cry11Aa and Cyt1Aa exhibit different structural orders in crystal topography

Chen

Teulon

Pellequer

2023

J of Molecular Recognition

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Cry11Aa and Cyt1Aa are two pesticidal toxins produced by Bacillus thuringiensis subsp. israelensis. To improve our understanding of the nature of their oligomers in the toxic actions and synergistic effects, we performed the atomic force microscopy to probe the surfaces of their natively grown crystals, and used the L‐weight filter to enhance the structural features. By L‐weight filtering, molecular sizes of the Cry11Aa and Cyt1Aa monomers obtained are in excellent agreement with the three‐dimensional structures determined by x‐ray crystallography. Moreover, our results show that the layered feature of a structural element distinguishes the topographic characteristics of Cry11Aa and Cyt1Aa crystals, suggesting that the Cry11Aa toxin has a better chance than Cyt1Aa for multimerization and therefore cooperativeness of the toxic actions.

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“…The first discovered microbial rhodopsins (M-Rho) are typically seven-pass transmembrane helix region bound with retinal to absorb light energy for ion translocation or phototaxis response [ 4 , 5 ]. The photochemical properties of ion-translocating rhodopsins fall into several categories, such as the light-driven outward proton transport bacteriorhodopsin (BR) [ 4 , 6 ], the light-driven inward chloride transport halorhodopsin (HR) [ 7 , 8 ], outward sodium transport (KR2) [ 9 ], and the nonselective cation channel channelrhodopsin II (ChR2) [ 10 , 11 ].…”

Section: Introductionmentioning

confidence: 99%

Engineered Bacteriorhodopsin May Induce Lung Cancer Cell Cycle Arrest and Suppress Their Proliferation and Migration

Wong

Huang

et al. 2021

Molecules

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Highly expressible bacteriorhodopsin (HEBR) is a light-triggered protein (optogenetic protein) that has seven transmembrane regions with retinal bound as their chromophore to sense light. HEBR has controllable photochemical properties and regulates activity on proton pumping. In this study, we generated HEBR protein and incubated with lung cancer cell lines (A549 and H1299) to evaluate if there was a growth-inhibitory effect with or without light illumination. The data revealed that the HEBR protein suppressed cell proliferation and induced the G0/G1 cell cycle arrest without light illumination. Moreover, the migration abilities of A549 and H1299 cells were reduced by ~17% and ~31% after incubation with HEBR (40 μg/mL) for 4 h. The Snail-1 gene expression level of the A549 cells was significantly downregulated by ~50% after the treatment of HEBR. In addition, HEBR significantly inhibited the gene expression of Sox-2 and Oct-4 in H1299 cells. These results suggested that the HEBR protein may inhibit cell proliferation and cell cycle progression of lung cancer cells, reduce their migration activity, and suppress some stemness-related genes. These findings also suggested the potential of HEBR protein to regulate the growth and migration of tumor cells, which may offer the possibility for an anticancer drug.

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Insertion and activation of functional Bacteriorhodopsin in a floating bilayer

Cited by 4 publications

References 67 publications

Probing the Separation Distance between Biological Nanoparticles and Cell Membrane Mimics Using Neutron Reflectometry with Sub-Nanometer Accuracy

Probing the Separation Distance between Biological Nanoparticles and Cell Membrane Mimics Using Neutron Reflectometry with Sub-Nanometer Accuracy

Cry11Aa and Cyt1Aa exhibit different structural orders in crystal topography

Engineered Bacteriorhodopsin May Induce Lung Cancer Cell Cycle Arrest and Suppress Their Proliferation and Migration

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