Detection of Carbendazim by Surface-Enhanced Raman Scattering Using Cyclodextrin Inclusion Complexes on Gold Nanorods

Strickland, Aaron D.; Batt, Carl A.

doi:10.1021/ac801626x

Cited by 135 publications

(70 citation statements)

References 47 publications

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“…A 10 µL aliquot of the protein solution was applied to a Renishaw InVia micro-Raman spectrophotometer using long-range 50× objective, 30sec. integration, and 10% laser power (785 nm excitation; 8 mW at 100%) [49]. The spectra were corrected by subtracting the buffer and background.…”

Section: Methodsmentioning

confidence: 99%

The Terminal Immunoglobulin-Like Repeats of LigA and LigB of Leptospira Enhance Their Binding to Gelatin Binding Domain of Fibronectin and Host Cells

et al. 2010

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Leptospira spp. are pathogenic spirochetes that cause the zoonotic disease leptospirosis. Leptospiral immunoglobulin (Ig)-like protein B (LigB) contributes to the binding of Leptospira to extracellular matrix proteins such as fibronectin, fibrinogen, laminin, elastin, tropoelastin and collagen. A high-affinity Fn-binding region of LigB has been localized to LigBCen2, which contains the partial 11th and full 12th Ig-like repeats (LigBCen2R) and 47 amino acids of the non-repeat region (LigBCen2NR) of LigB. In this study, the gelatin binding domain of fibronectin was shown to interact with LigBCen2R (KD = 1.91±0.40 µM). Not only LigBCen2R but also other Ig-like domains of Lig proteins including LigAVar7'-8, LigAVar10, LigAVar11, LigAVar12, LigAVar13, LigBCen7'-8, and LigBCen9 bind to GBD. Interestingly, a large gain in affinity was achieved through an avidity effect, with the terminal domains, 13th (LigA) or 12th (LigB) Ig-like repeat of Lig protein (LigAVar7'-13 and LigBCen7'-12) enhancing binding affinity approximately 51 and 28 fold, respectively, compared to recombinant proteins without this terminal repeat. In addition, the inhibited effect on MDCKs cells can also be promoted by Lig proteins with terminal domains, but these two domains are not required for gelatin binding domain binding and cell adhesion. Interestingly, Lig proteins with the terminal domains could form compact structures with a round shape mediated by multidomain interaction. This is the first report about the interaction of gelatin binding domain of Fn and Lig proteins and provides an example of Lig-gelatin binding domain binding mediating bacterial-host interaction.

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Section: Methodsmentioning

confidence: 99%

The Terminal Immunoglobulin-Like Repeats of LigA and LigB of Leptospira Enhance Their Binding to Gelatin Binding Domain of Fibronectin and Host Cells

et al. 2010

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“…The development of strategies for the selective chemical functionalization of CDs has allowed the elaboration of nanoarchitectures engineered to perform a variety of tasks, e.g. targeting [26], sensing [27] or catalysis [28]. Nevertheless, the most relevant research in the field of CD-based nanoaggregates relay on synthetic methodologies which results in heterogeneous products [21].…”

Section: Introductionmentioning

confidence: 99%

Monodisperse Nanoparticles from Self-Assembling Amphiphilic Cyclodextrins: Modulable Tools for the Encapsulation and Controlled Release of Pharmaceuticals

Méndez‐Ardoy¹,

Gómez-Garcı́a²,

Gèze³

et al. 2012

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Selective chemical functionalization of cyclodextrins (CDs) is a readily amenable methodology to produce amphiphilic macromolecules endowed with modulable self-organizing capabilities. Herein, the synthesis of well-defined amphiphilic CD derivatives, with a "skirt-type" architecture, that incorporate long-chain fatty esters at the secondary hydroxyl rim and a variety of chemical functionalities (e. g. iodo, bromo, azido, cysteaminyl or isothiocyanato) at the primary hydroxyls rim is reported. Nanoprecipitation of the new CD facial amphiphiles, or binary mixtures of them, resulted in nanoparticles with average hydrodynamic diameters ranging from 100 to 240 nm that were stable in suspension for several months. The precise size, zeta potential and topology of the nanoparticles are intimately dependent on the functionalization pattern at the CD scaffold. Highly efficient molecular encapsulation capabilities of poorly bioavailable drugs such as diazepam (DZ) were demonstrated for certain derivatives, the drug release profile being dependent on the type of formulation (nanospheres or nanocapsules). The efficiency and versatility of the synthetic strategy, together with the possibility of exploiting the reactivity of the functional groups at the nanoparticle surface, offer excellent opportunities to further manipulate the carrier capabilities of this series of amphiphilic CDs from a bottom-up approach.

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“…[16][17][18] We demonstrated how to graft β-CD as an alkyl iodide derivative for reduced Cys under moderate conditions. The products were directly applied to spectroscopic and matrix-assisted laser desorption/ionization linear time-of-flight mass spectrometry (MALDI-TOF MS) analysis to confirm the conjugation.…”

Section: Introductionmentioning

confidence: 99%

Simple Preparation of Green Fluorescent Protein Conjugated with β-Cyclodextrin in a Site Specific Manner

et al. 2013

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We have site-directedly linked a green fluorescent protein (GFP) variant and a β-cyclodextrin (β-CD) with a simple method to develop a basic complex for sophisticated supramolecules. We have confirmed β-CD grafting on GFP with several methods including matrix-assisted laser desorption/ionization linear time-of-flight mass spectrometry (MALDI-TOF MS) without protease digestion and characterized the complex as well. In consideration of the resulting properties, the product we plainly and efficiently obtained could have applications related to sensing devices and drug delivery systems.

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Detection of Carbendazim by Surface-Enhanced Raman Scattering Using Cyclodextrin Inclusion Complexes on Gold Nanorods

Cited by 135 publications

References 47 publications

The Terminal Immunoglobulin-Like Repeats of LigA and LigB of Leptospira Enhance Their Binding to Gelatin Binding Domain of Fibronectin and Host Cells

The Terminal Immunoglobulin-Like Repeats of LigA and LigB of Leptospira Enhance Their Binding to Gelatin Binding Domain of Fibronectin and Host Cells

Monodisperse Nanoparticles from Self-Assembling Amphiphilic Cyclodextrins: Modulable Tools for the Encapsulation and Controlled Release of Pharmaceuticals

Simple Preparation of Green Fluorescent Protein Conjugated with β-Cyclodextrin in a Site Specific Manner

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