Multiplexed Plasmon Sensor for Rapid Label-Free Analyte Detection

Rosman, Christina; Prasad, Janak; Neiser, A.; Henkel, Andreas; Edgar, J.A.; Sönnichsen, Carsten

doi:10.1021/nl401354f

Cited by 105 publications

(117 citation statements)

References 25 publications

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“…Gold Nanorod Preparation, Characterization, and Coating with Lipids-CTAB-AuNRs were synthesized and characterized as described previously (34). The particles used here showed a refractive index sensitivity S ϭ d/dn of S ϭ (143.1 Ϯ 39.5) nm/RIU (if immobilized on a surface), and their dimensions determined by electron microscopy were: diameter d ϭ (31.1 Ϯ 5.6) nm; length l ϭ 67.8 Ϯ 9.2 nm.…”

Section: Methodsmentioning

confidence: 99%

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Organization into Higher Ordered Ring Structures Counteracts Membrane Binding of IM30, a Protein Associated with Inner Membranes in Chloroplasts and Cyanobacteria

Heidrich

Wulf

Hennig

et al. 2016

Journal of Biological Chemistry

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The IM30 (inner membrane-associated protein of 30 kDa), also known as the Vipp1 (vesicle-inducing protein in plastids 1), has a crucial role in thylakoid membrane biogenesis and maintenance. Recent results suggest that the protein binds peripherally to membranes containing negatively charged lipids. However, although IM30 monomers interact and assemble into large oligomeric ring complexes with different numbers of monomers, it is still an open question whether ring formation is crucial for membrane interaction. Here we show that binding of IM30 rings to negatively charged phosphatidylglycerol membrane surfaces results in a higher ordered membrane state, both in the head group and in the inner core region of the lipid bilayer. Furthermore, by using gold nanorods covered with phosphatidylglycerol layers and single particle spectroscopy, we show that not only IM30 rings but also lower oligomeric IM30 structures interact with membranes, although with higher affinity. Thus, ring formation is not crucial for, and even counteracts, membrane interaction of IM30.Engulfment of an ancient cyanobacterium by a primordial cell has resulted in the development of modern day chloroplasts, the organelles where photosynthesis takes place. Consequently, the fine structures of cyanobacterial cells and chloroplasts share many similarities. Notably, chloroplasts and cyanobacteria both contain an extra internal membrane system, the thylakoid membrane (TM) 2 network. Furthermore, both perform oxygenic photosynthesis, and the TMs harbor all protein complexes and pigments involved in the photosynthetic light reaction. However, although assembly and maintenance of TMs is vital for photosynthesis, the details of TM biogenesis and maintenance are still largely unsolved mysteries (1).In 1994 the IM30 (inner membrane-associated protein of 30 kDa) was discovered in chloroplasts of Pisum sativum (2), and a homologous protein appears to be expressed in almost every organism that is able to conduct oxygenic photosynthesis (2-5). Several in vivo studies have shown that the protein plays an essential role in TM formation and maintenance (reviewed in Ref. 6), e.g. the depletion of the protein in Arabidopsis thaliana or the cyanobacterium Synechocystis sp. PCC 6803 has resulted in a decreased amount of TMs (3, 7-9). Under cold stress conditions, depletion of IM30 resulted in the formation of vesicular structures at the chloroplast inner envelope membrane in Arabidopsis, which led to the name Vipp1 (vesicle inducing protein in plastids 1) (3). Nevertheless, although diverse physiological functions were proposed for IM30 in the past two decades, the exact protein function remained elusive for a long time. Only recently, IM30 has been identified to be able to reorganize lipid bilayer structures and to mediate membrane fusion in chloroplasts and cyanobacteria (10). Similar to its bacterial homolog, the PspA (phage shock protein A), which is involved in a bacterial stress response in situations provoking membrane stress (11), IM30 specifically interacts wi...

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Section: Methodsmentioning

confidence: 99%

“…The optical dark field spectroscopy setup used to record single particle spectra was described in detail previously (34). AuNRs, immobilized on the glass surface of a flow cell, were illuminated by dark field illumination so that only the scattered light of a single nanoparticle entered the spectrometer at a given time.…”

Section: Methodsmentioning

confidence: 99%

Organization into Higher Ordered Ring Structures Counteracts Membrane Binding of IM30, a Protein Associated with Inner Membranes in Chloroplasts and Cyanobacteria

Heidrich

Wulf

Hennig

et al. 2016

Journal of Biological Chemistry

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“…The plasmonic properties of gold nanorods allow them to be used in photothermal therapy [1,2], imaging techniques [3,4], theranostics [5,6], sensing applications [7][8][9][10] and optical memories [11,12].…”

Section: Introductionmentioning

confidence: 99%

Thermal stability of mesoporous silica-coated gold nanorods with different aspect ratios

Gergely-Fülöp

Zámbó

Deák

2014

Materials Chemistry and Physics

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The effect of different temperatures (up to 900 °C) on the morphology of mesoporous silicacoated gold nanorods was systematically investigated. Gold nanorods with different aspect ratios (AR ranging from 2.5 to 4.3) were coated with a 15 nm thick mesoporous silica shell.Silicon supported monolayers of the particles were annealed in the temperature range of 300-900 °C. The resulting changes in particle morphology were investigated using scanning electron microscopy and visible wavelength extinction spectroscopy. The silica coating generally improved the stability of the nanorods from ca. 250 °C by several hundreds degree Celsius. For nanorods with AR<3 the shape and the aspect ratio change is only moderate up to 700 °C. At 900 °C these nanorods became spherical. For nanorods with AR>3, lower stability was found as the aspect ratio decrease was more significant and they transformed into spherical particles already at 700 °C. It was confirmed by investigating empty silica shells that the observed conformal change of the shell material when annealing core/shell particles is dictated by the deformation of the core particle. This also implies that a significant mechanical stress is exerted on the shell upon core deformation. In accordance with this, for the highest aspect ratio (AR~4) nanorod the shell breaks up at 900 °C and the gold cores were partially released and coalesced into large spherical particles.

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“…In this sense, Sönnichsen and co-workers have detected single unlabeled proteins with extremely high temporal resolution, allowing for monitoring the dynamic evolution of proteins [48]. In an advanced design, the same group has developed an efficient and cost-effective multiplexed sensor for proteins, in which the LSPR position of rod-shape AuNPs responds specifically to different proteins [49]. The efficiency of this original method lies in the nanomolar sensitivity, the sensor recycling capability, and the potential to upscale to hundreds of targets.…”

Section: Lspr-based Nanosensing Using Colloidal Metal Nps On Substratesmentioning

confidence: 99%

Recent progress on colloidal metal nanoparticles as signal enhancers in nanosensing

Abalde‐Cela

Carregal‐Romero

Coelho

et al. 2016

Advances in Colloid and Interface Science

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Multiplexed Plasmon Sensor for Rapid Label-Free Analyte Detection

Cited by 105 publications

References 25 publications

Organization into Higher Ordered Ring Structures Counteracts Membrane Binding of IM30, a Protein Associated with Inner Membranes in Chloroplasts and Cyanobacteria

Organization into Higher Ordered Ring Structures Counteracts Membrane Binding of IM30, a Protein Associated with Inner Membranes in Chloroplasts and Cyanobacteria

Thermal stability of mesoporous silica-coated gold nanorods with different aspect ratios

Recent progress on colloidal metal nanoparticles as signal enhancers in nanosensing

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