Plasmon Waveguide Resonance Research Articles

Self-Referenced Plasmon Waveguide Resonance Sensor Using Different Waveguide Modes

We report a plasmon waveguide resonance (PWR) sensing structure supporting two waveguide modes for self-referenced measurement. We show theoretically the dual mode PWR sensing structure owns unique opportunities for self-referenced measurement, and the accuracy and cross sensitivity can be optimized by simply varying the gold film thickness or dielectric layer thickness or dielectric film refractive index. This structure may provide an approach owning good compatibility with the surface plasmon resonance and PWR biosensors for self-referenced biosensing.

Using Surface Plasmon Resonance to Study Species Transport across Lipid Membranes

Studying species transport across lipid membranes by membrane transport proteins is important for various biological applications. Although patch-clamp technique is well developed for recording the ion transport across lipid membranes, the technique requires well trained personals for the challenging and delicate operation. In this study, we demonstrated using the surface plasmon resonance (SPR) based platform to detect the concentration change of the target species across the lipid membrane. We created sub-micron sized pore structure on the platform, in which the bottom surface is gold and the top surface is silica, and spanned lipid membranes over the pore. The process created a space inside the pore separated from the outside environment by the free-standing lipid membrane for further studying the species transport across the membrane. The platform geometry allowed us to combine plasmon-waveguide resonance (PWR) to the system to simultaneously monitor the refractive index change in the pore space, which is correlated to the target species concentration, and the refractive index change on the membrane above the top silica surface, which is correlated to the binding events occurring on the membrane surface. We expect to use this platform to monitor how various inhibitors or ligands could influence the transport dynamic of interested membrane transport proteins.

Spectral Splitting Based on Electromagnetically Induced Transparency in Plasmonic Waveguide Resonator System

Spectral splitting is numerically investigated based on the electromagnetically induced transparency (EIT) in a nanoscale plasmonic waveguide resonator system, which consists of a square ring resonator coupled with a stub-shaped metal-insulator-metal (MIM) waveguide. Simulation results show that the transparency window can be easily tuned by changing the geometrical parameters of the structure and the material filled in the resonators. By adding another stub or (and) square ring resonator, multi-EIT-like peaks appear in the broadband transmission spectrum, and the physical mechanism is presented. Our compact plasmonic structure may have potential applications for nanoscale optical switching, nanosensor, nanolaser, and slow-light devices in highly integrated optical circuits.

Fourier transform-plasmon waveguide spectroscopy: a nondestructive multifrequency method for simultaneously determining polymer thickness and apparent index of refraction.

Fourier transform (FT)-plasmon waveguide resonance (PWR) spectroscopy measures light reflectivity at a waveguide interface as the incident frequency and angle are scanned. Under conditions of total internal reflection, the reflected light intensity is attenuated when the incident frequency and angle satisfy conditions for exciting surface plasmon modes in the metal as well as guided modes within the waveguide. Expanding upon the concept of two-frequency surface plasmon resonance developed by Peterlinz and Georgiadis [Opt. Commun. 1996, 130, 260], the apparent index of refraction and the thickness of a waveguide can be measured precisely and simultaneously by FT-PWR with an average percent relative error of 0.4%. Measuring reflectivity for a range of frequencies extends the analysis to a wide variety of sample compositions and thicknesses since frequencies with the maximum attenuation can be selected to optimize the analysis. Additionally, the ability to measure reflectivity curves with both p- and s-polarized light provides anisotropic indices of refraction. FT-PWR is demonstrated using polystyrene waveguides of varying thickness, and the validity of FT-PWR measurements are verified by comparing the results to data from profilometry and atomic force microscopy (AFM).

Multiple Fano Resonances Based on Different Waveguide Modes in a Symmetry Breaking Plasmonic System

Multiple Fano resonances are numerically investigated based on different waveguide modes in a nanoscale plasmonic waveguide resonator system, which consists of two grooves coupled with a metal-insulator-metal (MIM) waveguide. Simulation results show that by introducing a small structural breaking in the plasmonic resonator, both symmetric and antisymmetric waveguide modes can be excited. Due to the interaction of the symmetric and antisymmetric waveguide modes, the transmission spectra possess a sharp asymmetrical profile. Because of different origins, these Fano resonances exhibit different dependence on the parameters of the structure and can be easily tuned. These characteristics offer flexibility to design the device. This nanosensor yields a sensitivity of ~820 nm/RIU and a figure-of-merit of ~ 3.2× 10 <sup xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink">5</sup> . The utilization of the antisymmetric mode in the MIM waveguide provides a new possibility for designing high-performance plasmonic devices.

The role of tryptophans on the cellular uptake and membrane interaction of arginine-rich cell penetrating peptides

Cell-penetrating peptides (CPP) are able to efficiently transport cargos across cell membranes without being cytotoxic to cells, thus present a great potential in drug delivery and diagnosis. While the role of cationic residues in CPPs has been well studied, that of Trp is still not clear. Herein 7 peptide analogs of RW9 (RRWWRRWRR, an efficient CPP) were synthesized in which Trp were systematically replaced by Phe residues. Quantification of cellular uptake reveals that substitution of Trp by Phe strongly reduces the internalization of all peptides despite the fact that they strongly accumulate in the cell membrane. Cellular internalization and biophysical studies show that not only the number of Trp residues but also their positioning in the helix and the size of the hydrophobic face they form are important for their internalization efficacy, the highest uptake occurring for the analog with 3 Trp residues. Using CD and ATR-FTIR spectroscopy we observe that all peptides became structured in contact with lipids, mainly in α-helix. Intrinsic tryptophan fluorescence studies indicate that all peptides partition in the membrane in about the same manner (Kp~105) and that they are located just below the lipid headgroups (~10Å) with slightly different insertion depths for the different analogs. Plasmon Waveguide Resonance studies reveal a direct correlation between the number of Trp residues and the reversibility of the interaction following membrane washing. Thus a more interfacial location of the CPP renders the interaction with the membrane more adjustable and transitory enhancing its internalization ability.

Plasmon waveguide resonance sensor using an Au-MgF2 structure.

We report an Au − MgF(2) plasmon waveguide resonance (PWR) sensor in this work. The characteristics of this sensing structure are compared with a surface plasmon resonance (SPR) structure theoretically and experimentally. The transverse-magnetic-polarized PWR sensor has a refractive index resolution of 9.3 × 10(-7) RIU, which is 6 times smaller than that of SPR at the incident light wavelength of 633 nm, and the transverse-electric-polarized PWR sensor has a refractive index resolution of 3.0 × 10(-6) RIU. This high-resolution sensor is easy to build and is less sensitive to film coating deviations.

Self-referenced spectroscopy using plasmon waveguide resonance biosensor.

A plasmon waveguide resonance (PWR) sensor is designed, fabricated, and tested for self-referenced biosensing. The PWR sensor is able to support two different polarizations, TM and TE. The TM polarization has a large sensitivity to variations in the background refractive index while the TE polarization is more sensitive to the surface properties. The ability of the PWR sensor to simultaneously operate in both TM and TE modes is used to decouple the background index variations (bulk effects) from the changes in adlayer thickness (surface effects) via multimode spectroscopy. To benchmark the performance of the PWR, a conventional surface plasmon resonance (SPR) sensor is fabricated and tested under the same conditions.

A peptide derived from the rotavirus outer capsid protein VP7 permeabilizes artificial membranes

Biological membranes represent a physical barrier that most viruses have to cross for replication. While enveloped viruses cross membranes through a well-characterized membrane fusion mechanism, non-enveloped viruses, such as rotaviruses, require the destabilization of the host cell membrane by processes that are still poorly understood. We have identified, in the C-terminal region of the rotavirus glycoprotein VP7, a peptide that was predicted to contain a membrane domain and to fold into an amphipathic α-helix. Its structure was confirmed by circular dichroism in media mimicking the hydrophobic environment of the membrane at both acidic and neutral pHs. The helical folding of the peptide was corroborated by ATR-FTIR spectroscopy, which suggested a transmembrane orientation of the peptide. The interaction of this peptide with artificial membranes and its affinity were assessed by plasmon waveguide resonance. We have found that the peptide was able to insert into membranes and permeabilize them while the native protein VP7 did not. Finally, NMR studies revealed that in a hydrophobic environment, this helix has amphipathic properties characteristic of membrane-perforating peptides. Surprisingly, its structure varies from that of its counterpart in the structure of the native protein VP7, as was determined by X-ray. All together, our results show that a peptide released from VP7 is capable of changing its conformation and destabilizing artificial membranes. Such peptides could play an important role by facilitating membrane crossing by non-enveloped viruses during cell infection.

Probing the kinetics of lipid membrane formation and the interaction of a nontoxic and a toxic amyloid with plasmon waveguide resonance

The kinetics of formation of solid-supported lipid model membranes were investigated using a home-made plasmon waveguide resonance (PWR) sensor possessing enhanced properties relative to classic surface plasmon resonance sensors. Additionally, the kinetics of interaction of two amyloid peptides with zwitterionic and anionic membranes and their effect on lipid organization were followed.

A BIOSENSOR USING COUPLED PLASMON WAVEGUIDE RESONANCE COMBINED WITH HYPERSPECTRAL FLUORESCENCE ANALYSIS

We developed a biosensor that is capable for simultaneous surface plasmon resonance (SPR) sensing and hyperspectral fluorescence analysis in this paper. A symmetrical metal-dielectric slab scheme is employed for the excitation of coupled plasmon waveguide resonance (CPWR) in the present work. Resonance between surface plasmon mode and the guided waveguide mode generates narrower full width half-maximum of the reflective curves which leads to increased precision for the determination of refractive index over conventional SPR sensors. In addition, CPWR also offers longer surface propagation depths and higher surface electric field strengths that enable the excitation of fluorescence with hyperspectral technique to maintain an appreciable signal-to-noise ratio. The refractive index information obtained from SPR sensing and the chemical properties obtained through hyperspectral fluorescence analysis confirm each other to exclude false-positive or false-negative cases. The sensor provides a comprehensive understanding of the biological events on the sensor chips.

Multi-Channel Hyperspectral Fluorescence Detection Excited by Coupled Plasmon-Waveguide Resonance

We propose in this paper a biosensor scheme based on coupled plasmon-waveguide resonance (CPWR) excited fluorescence spectroscopy. A symmetrical structure that offers higher surface electric field strengths, longer surface propagation lengths and depths is developed to support guided waveguide modes for the efficient excitation of fluorescence. The optimal parameters for the sensor films are theoretically and experimentally investigated, leading to a detection limit of 0.1 nM (for a Cy5 solution). Multiplex analysis possible with the fluorescence detection is further advanced by employing the hyperspectral fluorescence technique to record the full spectra for every pixel on the sample plane. We demonstrate experimentally that highly overlapping fluorescence (Cy5 and Dylight680) can be distinguished and ratios of different emission sources can be determined accurately. This biosensor shows great potential for multiplex detections of fluorescence analytes.

Rubber particle proteins, HbREF and HbSRPP, show different interactions with model membranes

The biomembrane surrounding rubber particles from the hevea latex is well known for its content of numerous allergen proteins. HbREF (Hevb1) and HbSRPP (Hevb3) are major components, linked on rubber particles, and they have been shown to be involved in rubber synthesis or quality (mass regulation), but their exact function is still to be determined. In this study we highlighted the different modes of interactions of both recombinant proteins with various membrane models (lipid monolayers, liposomes or supported bilayers, and multilamellar vesicles) to mimic the latex particle membrane. We combined various biophysical methods (polarization-modulation-infrared reflection-adsorption spectroscopy (PM-IRRAS)/ellipsometry, attenuated-total reflectance Fourier-transform infrared (ATR-FTIR), solid-state nuclear magnetic resonance (NMR), plasmon waveguide resonance (PWR), fluorescence spectroscopy) to elucidate their interactions. Small rubber particle protein (SRPP) shows less affinity than rubber elongation factor (REF) for the membranes but displays a kind of “covering” effect on the lipid headgroups without disturbing the membrane integrity. Its structure is conserved in the presence of lipids. Contrarily, REF demonstrates higher membrane affinity with changes in its aggregation properties, the amyloid nature of REF, which we previously reported, is not favored in the presence of lipids. REF binds and inserts into membranes. The membrane integrity is highly perturbed, and we suspect that REF is even able to remove lipids from the membrane leading to the formation of mixed micelles. These two homologous proteins show affinity to all membrane models tested but neatly differ in their interacting features. This could imply differential roles on the surface of rubber particles.

An improved refractive index sensor based on genetic optimization of plasmon waveguide resonance

Plasmon waveguide resonance (PWR) sensors are particularly useful for biosensing due to their unique ability to perform sensing with two different polarizations. In this paper we report a comprehensive performance comparison between the surface plasmon resonance (SPR) sensor and the PWR sensor in terms of the sensitivity and the refractive index resolution. Both sensors were optimized using a genetic algorithm to acquire their best performance for bulk sensing applications. The experimental results show that the PWR sensor has a refractive index resolution of 5 × 10(-7) RIU which is 6 times smaller than that of the optimized SPR sensor. The TE polarization in the PWR sensor has a resolution of 1.4 × 10(-6) RIU which is smaller than the SPR sensor. The polarization diversity in the PWR sensor is another advantage which can be used to improve the measurement reliability.

Isoniazid interaction with phosphatidylcholine-based membranes

Interaction between the anti-tuberculosis drug isoniazid (INH) and phosphatidylcholine membranes was investigated in terms of: (i) drug affinity to a lipid bilayer and (ii) drug-induced changes in the dynamic properties of liposomes, such as membrane hydration state, polar head and non-polar acyl chain order and lipid phase transition behavior. These parameters were studied by plasmon waveguide resonance spectroscopy (PWR), UV–visible, horizontal attenuated total reflectance–Fourier transform infrared (HATR–FTIR), nuclear magnetic resonance (NMR) and differential scanning calorimetry (DSC) techniques. PWR measurements showed an INH membrane dissociation constant value of 0.031μM to phosphatidylcholine bilayers. INH induced higher membrane perturbation in the plane which is perpendicular to the membrane plane. The INH saturation concentration in phosphatidylcholine liposomes was 170μM. At this concentration, HATR–FTIR and NMR findings showed that INH may interact with the lipid polar head, increasing the number of hydrogen bonds in the phosphate region and enhancing the choline motional freedom. DSC measurements showed that, at 115μM, INH was responsible for a decrease in lipid phase transition temperature of approximately 2°C and had no influence in the lipid enthalpy variation (ΔH). However, at 170μM, INH induced the reduction of the ΔH by approximately 52%, suggesting that the drug may increase the distance among lipid molecules and enhance the freedom of the lipid acyl chains methylene groups. This paper provides information on the effects of INH on membrane dynamics which is important to understand liposome targeting of the drug and for the development of anti-TB pharmacologic systems that not only are less susceptible to resistance but also have low toxicity.

Plasmon Waveguide Resonance Raman Spectroscopy

Raman spectra were collected from a 1.25 M aqueous pyridine solution, 100-nm polystyrene film or a trimethyl(phenyl)silane monolayer at a plasmon waveguide interface under total internal reflection (TIR). The plasmon waveguide resonance (PWR) interface consisted of a sapphire prism/49 to 50 nm Au/548 to 630 nm SiO(2) and a monolayer, thin film or aqueous analyte. The Raman peak area as a function of incident angle was measured using a 785-nm excitation wavelength, and was compared to the Raman peak area obtained at a sapphire or sapphire/50 nm Au interface. In contrast to measurements at a bare sapphire prism, increased surface sensitivity and signal were obtained from the PWR interface. In contrast to measurements at a bare Au film where only p-polarized incident light generates an enhanced interfacial electric field, plasmon waveguide interfaces enable excitation with orthogonal polarizations using s- or p-polarized incident light. The Raman scatter from a monolayer was recorded at the PWR interface with a signal-to-noise ratio of 5.6 when averaging 3 accumulations with 3 min acquisition times using nonresonant excitation, whereas no signal was recorded from a monolayer at the sapphire interface. The reflected light from the interface enabled the identification of the incident angle where the maximum Raman scatter was produced, and the Raman signal generated at the plasmon waveguide interface was modeled by the enhanced interfacial mean square electric field relative to the incident field. In comparison to the techniques on which this work was based (i.e., PWR spectroscopy, TIR Raman spectroscopy at the prism interface, and surface plasmon resonance (SPR) Raman spectroscopy at the prism/Au interface), chemical specificity was added to PWR spectroscopy, a signal enhancement mechanism was introduced for TIR Raman spectroscopy, and polarization control of the interfacial electric field was added to SPR Raman spectroscopy.

Coupled plasmonic assisted progressive multiple resonance for dielectric material characterization

In this paper, we report the theoretical analysis of different types of plasmonic structures with the main emphasis on the coupled plasmon waveguide resonance due to several advantages offered by the same compared to other structures. Multiple resonance dips are found to increase with the increase in the dielectric layer thickness and this progressive nature of the dips can be efficiently utilized to characterize the dielectric material within a composite multilayer plasmonic structure. Supporting simulation results carried out in the MATLAB environment are also provided to validate the proposed application.

Sensitivity comparison of surface plasmon resonance and plasmon-waveguide resonance biosensors

Plasmon-waveguide resonance (PWR) sensors are particularly useful for the investigation of biomolecular interactions with or within lipid bilayer membranes. Many studies demonstrated their ability to provide unique qualitative information, but the evaluation of their sensitivity as compared to other surface plasmon resonance (SPR) sensors has not been broadly investigated. We report here a comprehensive sensitivity comparison of SPR and PWR biosensors for the p-polarized light component. The sensitivity of five different biosensor designs to changes in refractive index, thickness and mass are determined and discussed. Although numerical simulations show an increase of the electric field intensity by 30–35% and the penetration depth by four times in PWR, the waveguide-based method is 0.5–8-fold less sensitive than conventional SPR in all considered analytical parameters. The experimental results also suggest that the increase in the penetration depth in PWR is made at the expense of the surface sensitivity. The physical and structural reasons for PWR sensor limitations are discussed and a general viewpoint for designing more efficient SPR sensors based on dielectric slab waveguides is provided.

NMR Structure of a Viral Peptide Inserted in Artificial Membranes: A VIEW ON THE EARLY STEPS OF THE BIRNAVIRUS ENTRY PROCESS

Nonenveloped virus must penetrate the cellular membrane to access the cytoplasm without the benefit of membrane fusion. For birnavirus, one of the peptides present in the virus capsid, pep46 for infectious bursal disease virus, is able to induce pores into membranes as an intermediate step of the birnavirus-penetration pathway. Using osmotic protection experiments, we demonstrate here that pep46 and its pore-forming N-terminal moiety (pep22) form pores of different diameters, 5-8 and 2-4 nm, respectively, showing that both pep46 moieties participate to pore formation. The solution structures of pep46, pep22, and pep24 (the pep46 C-terminal moiety) in different hydrophobic environments and micelles determined by (1)H NMR studies provide structural insights of the pep46 domain interaction. In CDCl(3)/CD(3)OH mixture and in dodecylphosphocholine micelles, the N-terminal domain of pep46 is structured in a long kinked helix, although the C terminus is structured in one or two helices depending upon the solvents used. We also show that the folding and the proline isomerization status of pep46 depend on the type of hydrophobic environment. NMR spectroscopy with labeled phospholipid micelles, differential scanning calorimetry, and plasmon waveguide resonance studies show the peptides lie parallel to the lipid-water interface, perturbing the fatty acid chain packing. All these data lead to a model in which the two domains of pep46 interact with the membrane to form pores.

The Role of Membranes in the Organization of HIV-1 Gag p6 and Vpr: p6 Shows High Affinity for Membrane Bilayers Which Substantially Increases the Interaction between p6 and Vpr.

The molecular mechanism by which HIV-1 Gag proteins are targeted and transported to the plasma membrane after ribosomal synthesis is unknown. In this work, we investigated the potential interaction of p6 and Vpr with model membranes and have determined their binding constants. Plasmon waveguide resonance (PWR) experiments showed that p6 strongly interacts with membranes (K(d) approximately 40 nM), which may help explaining in part why Gag is targeted to and assembles into membranes by coating itself with lipids. Moreover, a substantial increased affinity of Vpr for p6 was observed while in a membrane environment. In order to further investigate the molecular properties behind the high affinity to model membranes, molecular dynamics simulations were carried out for p6 with a dodecylphosphocholine (DPC) micelle. The results indicate an integration route model for Vpr into virions and may help explain why previous reports failed to detect p6 in virion core preparations.