Study of the Adsorption of 1,2,3-Triazole on Silver and Gold Colloidal Nanoparticles by Means of Surface Enhanced Raman Scattering

Pergolese, Barbara; Muniz‐Miranda, Maurizio; Bigotto, Adriano

doi:10.1021/jp0377228

Cited by 80 publications

(83 citation statements)

References 24 publications

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“…An important aspect of SERS is its potential in probing the interaction between various adsorbates and metallic surfaces [3][4][5][6][7][8][9][10][11][12][13][14]. Application of the 'surface selection rules' [15,16] provides information on the sites of binding and the molecular orientation on the metal surface.…”

Section: Introductionmentioning

confidence: 99%

Probing the adsorption mechanism in thiamazole bound to the silver surface with Surface-enhanced Raman Scattering and DFT

Biswas

Thomas

Sarkar

et al. 2009

Chemical Physics Letters

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Section: Introductionmentioning

confidence: 99%

Probing the adsorption mechanism in thiamazole bound to the silver surface with Surface-enhanced Raman Scattering and DFT

Biswas

Thomas

Sarkar

et al. 2009

Chemical Physics Letters

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“…In order to get a better insight into the adsorption mechanism of ANP on silver, DFT calculations of the harmonic vibrational frequencies of surface complexes formed by ANP À with silver adatoms have been carried out. In fact, these kinds of calculations are able to give useful information about the interaction between adsorbate and metal substrate; in particular, DFT calculations were previously employed successfully for other ligands like pyrazole [9], triazole [10,11] and pyridine [12]. Here, a combined SERS/DFT investigation is proposed for nitroarenes, by studying the adsorption of ANP in colloidal suspensions of silver nanoparticles.…”

Section: Introductionmentioning

confidence: 99%

SERS and DFT study of nitroarenes adsorbed on metal nanoparticles

Muniz‐Miranda¹,

Pergolese²,

Bigotto³

2007

Vibrational Spectroscopy

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“…Benzotriazole dyes adsorb onto silver nanoparticle surfaces in the same orientation irrespective of concentration, resulting in reproducible Raman spectral intensities (49). This is attributable to steric hindrance presented by covalent interactions between N 1 and N 3 lone electron pairs with the silver surface (50,51). BT has an absorbance λ max of 487 nm and, as such, is close in resonance when using an excitation wavelength of 514 nm.…”

Section: Resultsmentioning

confidence: 99%

Nanosensing protein allostery using a bivalent mouse double minute two (MDM2) assay

Robson

Hupp

Lickiss

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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The tumor suppressor protein, p53, is either mutated or absent in >50% of cancers and is negatively regulated by the mouse double minute (MDM2) protein. Understanding and inhibition of the MDM2-p53 interaction are, therefore, critical for developing novel chemotherapeutics, which are currently limited because of a lack of appropriate study tools. We present a nanosensing approach to investigate full-length MDM2 interactions with p53, thus providing an allosteric assay for identifying binding ligands. Surface-enhanced Raman scattering (SERS)-active nanoparticles, functionalized with a p53 peptide mimic (peptide 12.1), display biologically specific aggregation following addition of MDM2. Nanoparticle assembly is competitively inhibited by the N-terminal MDM2-binding ligands peptide 12.1 and Nutlin-3. This study reports nanoparticle assembly through specific protein-peptide interactions that can be followed by SERS. We demonstrate solution-based MDM2 allosteric interaction studies that use the full-length protein.assay system | biosensing | nano-assembly | protein interaction studies | Raman spectroscopyT he p53 tumor suppressor protein is often referred to as the "guardian of the genome" owing to its key role in cell-cycle regulation and its activity in a number of different cancer pathways (1-3). The antiproliferative action of p53 arises from the induction of cell-cycle arrest and apoptosis in cells subjected to DNA damage in response to stress. As such, p53 is central to protecting cells from uncontrolled growth and malignant transformation with inactivation or mutation of p53 found in over 50% of human cancers (1-3). Under nonstressed conditions, mouse double minute (MDM)2 negatively regulates p53, primarily through the ubiquitin degradation pathway but also via transrepression (4, 5). Studies have shown up-regulation of MDM2 in malignancies where p53 is fully functional, making the MDM2-p53 feedback loop of great interest in chemotherapeutic studies (6, 7).MDM2 is a multidomain protein that exerts E3-ligase activity on a number of proteins, including p53 (5, 8, 9). The ubiquitination activity of MDM2 is a multisubunit process whereby the N-terminal hydrophobic pocket and central acidic domain of MDM2 are used in p53 binding, to the N-terminal and central domains of p53, respectively (10). The complexity of this multisubunit interaction makes it relatively difficult to investigate the allosteric nature of MDM2. This is made more difficult by the problems in acquiring a structure of full-length MDM2 because of intrinsically disordered regions on the protein that reduce likelihood of crystallization. Focus solely on the N-terminal domain of MDM2 has identified Nutlin-3-type molecules that activate p53 in cells; however, these also act as allosteric agonists that stimulate rather than inhibit p53 ubiquitination (10-15). The putative dimerization of MDM2 through the C-terminal really interesting new gene (RING) domain is reported to be critical for E3-ligase activity; however, molecular reasoning for this is not f...

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Study of the Adsorption of 1,2,3-Triazole on Silver and Gold Colloidal Nanoparticles by Means of Surface Enhanced Raman Scattering

Cited by 80 publications

References 24 publications

Probing the adsorption mechanism in thiamazole bound to the silver surface with Surface-enhanced Raman Scattering and DFT

Probing the adsorption mechanism in thiamazole bound to the silver surface with Surface-enhanced Raman Scattering and DFT

SERS and DFT study of nitroarenes adsorbed on metal nanoparticles

Nanosensing protein allostery using a bivalent mouse double minute two (MDM2) assay

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