Plasmonic Nanosensors for the Determination of Drug Effectiveness on Membrane Receptors

Ahijado-Guzmán, Rubén; Menten, Julia; Prasad, Janak; Lambertz, Christina; Rivas, Germán; Sönnichsen, Carsten

doi:10.1021/acsami.6b14013

Cited by 10 publications

(8 citation statements)

References 29 publications

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“…We also confirmed the coverage of the nanoparticles with a lipid membrane by QCM and atomic force microscopy (Figure S12 and S13) in good agreement with results from plasmon spectroscopy, fluoresce microscopy, atomic force microscopy, and fluorescence recovery after photobleaching (FRAP) found in previous works. ,− , …”

Section: Resultssupporting

confidence: 90%

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Plasmonic Nanosensors Reveal a Height Dependence of MinDE Protein Oscillations on Membrane Features

Celiksoy

Jakab

et al. 2018

J. Am. Chem. Soc.

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Section: Resultssupporting

confidence: 90%

“…The gold nanorods were immobilized on one side of a microfluidic flow chamber and covered by a lipid membrane. The membrane deposition induced a notable plasmon wavelength shift Δλ (Figure b) . After addition of the Min proteins (MinD and MinE in buffer containing ATP), a patterned oscillation or wave forms on top of the lipid bilayer.…”

Section: Resultsmentioning

confidence: 99%

Plasmonic Nanosensors Reveal a Height Dependence of MinDE Protein Oscillations on Membrane Features

Celiksoy

Jakab

et al. 2018

J. Am. Chem. Soc.

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“…These observations already show interesting and previously inaccessible features such as a slow transition from periodic to chaotic behavior. It is straightforward to combine i-nSPR with nonimaging nanoSPR to obtain binding constants , and molecular distances, ,, which makes i-nSPR a versatile technique for biophysical studies of macromolecular interactions.…”

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confidence: 99%

Plasmonic Nanosensors for the Label-Free Imaging of Dynamic Protein Patterns

Celiksoy

Wandner

et al. 2020

J. Phys. Chem. Lett.

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We introduce a new approach to monitor the dynamics and spatial patterns of biological molecular assemblies. Our molecular imaging method relies on plasmonic gold nanoparticles as point-like detectors and requires no labeling of the molecules. We show spatial resolution of up to 5 μm and 30 ms temporal resolution, which is comparable to wide-field fluorescence microscopy, while requiring only readily available gold nanoparticles and a dark-field optical microscope. We demonstrate the method on MinDE proteins attaching to and detaching from lipid membranes of different composition for 24 h. We foresee our new imaging method as an indispensable tool in advanced molecular biology and biophysics laboratories around the world.

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“…Both particle batches led to similar signal/noise ratios, and their application in NanoSPR experiments resulted in similar K D values. To enable binding to the His-tagged protein receptors, the cetyl trimethylammonium bromide layer around the particles was replaced by NTA, and the His tags of the receptor proteins were complexed with nickel, adapting an established protocol (38).…”

Section: Preparation Characterization and Functionalization Of Goldmentioning

confidence: 99%

Structural and mechanistic insights into the interaction of the circadian transcription factor BMAL1 with the KIX domain of the CREB-binding protein

Garg

Orru

et al. 2019

Journal of Biological Chemistry

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Edited by Joel M. Gottesfeld The mammalian CLOCK:BMAL1 transcription factor complex and its coactivators CREB-binding protein (CBP)/p300 and mixed-lineage leukemia 1 (MLL1) critically regulate circadian transcription and chromatin modification. Circadian oscillations are regulated by interactions of BMAL1's C-terminal transactivation domain (TAD) with the KIX domain of CBP/p300 (activating) and with the clock protein CRY1 (repressing) as well as by the BMAL1 G-region preceding the TAD. Circadian acetylation of Lys 537 within the G-region enhances repressive BMAL1-TAD-CRY1 interactions. Here, we characterized the interaction of the CBP-KIX domain with BMAL1 proteins, including the BMAL1-TAD, parts of the G-region, and Lys 537. Tethering the small compound 1-10 in the MLL-binding pocket of the CBP-KIX domain weakened BMAL1 binding, and MLL1-bound KIX did not form a ternary complex with BMAL1, indicating that the MLL-binding pocket is important for KIX-BMAL1 interactions. Small-angle X-ray scattering (SAXS) models of BMAL1 and BMAL1:KIX complexes revealed that the N-terminal BMAL1 G-region including Lys 537 forms elongated extensions emerging from the bulkier BMAL1-TAD:KIX core complex. Fitting high-resolution KIX domain structures into the SAXS-derived envelopes suggested that the G-region emerges near the MLL-binding pocket, further supporting a role of this pocket in BMAL1 binding. Additionally, mutations in the second CREB-pKID/c-Myb-binding pocket of the KIX domain moderately impacted BMAL1 binding. The BMAL1(K537Q) mutation mimicking Lys 537 acetylation, however, did not affect the KIX-binding affinity, in contrast to its enhancing effect on CRY1 binding. Our results significantly advance the mechanistic understanding of the protein interaction networks controlling CLOCK:BMAL1-and CBP-dependent gene regulation in the mammalian circadian clock. Most organisms possess circadian rhythms coordinated by circadian clocks that synchronize them to the 24-h light-dark cycle. In mammals, circadian rhythmicity is controlled by transcriptional/translational feedback loops. The core transcriptional/translational feedback loop consists of the heterodimeric basic helix-loop-helix (bHLH) 4-PER-ARNT-SIM (PAS) domaincontaining transcriptional activators CLOCK (circadian locomotor output cycle kaput) and BMAL1 (brain and muscle ARNT-like protein-1), which circadianly regulate genes encoding Period (PER1, PER2, and PER3) and Cryptochrome (CRY1 and CRY2) clock proteins as well as many clock-controlled genes (1, 2). Analyses in mouse liver led to a model of three temporally separated states of CLOCK:BMAL1-dependent circadian transcription: an early repressive state, a late repressive state, and an active state (3). Large multisubunit PER-and CRY-containing complexes interact with CLOCK:BMAL1 in the early phase of repression (4), whereas CRY1 alone maintains the late repressive state (5, 6). In the active state, CLOCK:BMAL1 associates with co-activators such as the histone acetyl transferase CREB-binding protein (CBP) and its paralo...

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Plasmonic Nanosensors for the Determination of Drug Effectiveness on Membrane Receptors

Cited by 10 publications

References 29 publications

Plasmonic Nanosensors Reveal a Height Dependence of MinDE Protein Oscillations on Membrane Features

Plasmonic Nanosensors Reveal a Height Dependence of MinDE Protein Oscillations on Membrane Features

Plasmonic Nanosensors for the Label-Free Imaging of Dynamic Protein Patterns

Structural and mechanistic insights into the interaction of the circadian transcription factor BMAL1 with the KIX domain of the CREB-binding protein

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