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1.
Chem Commun (Camb) ; 54(65): 9067-9070, 2018 Aug 21.
Artigo em Inglês | MEDLINE | ID: mdl-30058653

RESUMO

This study focuses on the structural rearrangements and the photoluminescent behavior of pyrolytically derived carbon dots when subjected to a series of cyclic voltammetry sweeps. Although the electrical signals involved are not pronounced, multiple electrochemical cycling results in a progressive suppression of the photoluminescence, so that after 42 sweeps the intensity is reduced by one order of magnitude. At the same time, the fluorescence component stemming from the organic fluorophores is blue-shifted, while the contribution of the carbogenic cores is red-shifted. XPS and FTIR spectra reveal that the voltammetric field induces an extensive formation of C-O and C[double bond, length as m-dash]O at the expense of the C[double bond, length as m-dash]C bonds. Our findings indicate a close relationship between the electrochemical response and the structure of C-dots and, thus, have direct implications on the development of C-dot based electroluminescent materials, electrochemical sensors and solar cells.

2.
Chem Commun (Camb) ; 52(53): 8294-6, 2016 Jul 07.
Artigo em Inglês | MEDLINE | ID: mdl-27294695

RESUMO

Carbogenically coated silica nanoparticles (C-SiO2) exhibit color-tunability and carry great promise for two important forensic applications. First, the C-SiO2 nanopowders are ideal for fingerprint development, yielding strong contrast against multicoloured and patterned backgrounds. Second, spontaneous nanoparticle aggregation leads to non-duplicable, inexpensive nanotags that can support sustainable technologies to combat counterfeiting.

3.
Chem Commun (Camb) ; 51(23): 4902-5, 2015 Mar 21.
Artigo em Inglês | MEDLINE | ID: mdl-25704392

RESUMO

The incorporation of a minor amount of carbogenic nanoparticles into powder compositions imparts remarkable colour-tuneability, without compromising the flowability. In a proof-of-concept demonstration we report the use of these hybrid nanopowders for the visual enhancement of latent fingerprints where they effectively resolve issues arising from poor contrast against multi-coloured or patterned backgrounds.


Assuntos
Carbono/química , Nanopartículas/química , Pós/química , Dermatoglifia
4.
Langmuir ; 24(15): 8158-62, 2008 Aug 05.
Artigo em Inglês | MEDLINE | ID: mdl-18572891

RESUMO

The self-assembly of a modified fragment of the amyloid beta peptide, based on sequence Abeta(16-20), KLVFF, extended to give AAKLVFF is studied in methanol. Self-assembly into peptide nanotubes is observed, as confirmed by electron microscopy and small-angle X-ray scattering. The secondary structure of the peptide is probed by FTIR and circular dichroism, and UV/visible spectroscopy provides evidence for the important role of aromatic interactions between phenylalanine residues in driving beta-sheet self-assembly. The beta-sheets wrap helically to form the nanotubes, the nanotube wall comprising four wrapped beta-sheets. At higher concentration, the peptide nanotubes form a nematic phase that exhibits spontaneous flow alignment as observed by small-angle neutron scattering.


Assuntos
Metanol/química , Nanotubos de Peptídeos/química , Solventes/química , Dicroísmo Circular , Microscopia Eletrônica de Transmissão , Estrutura Molecular , Nanotubos de Peptídeos/ultraestrutura , Espectroscopia de Infravermelho com Transformada de Fourier
5.
Soft Matter ; 3(11): 1401-1406, 2007 Oct 16.
Artigo em Inglês | MEDLINE | ID: mdl-32900120

RESUMO

The self-assembly of a hydrophobically modified fragment of the amyloid ß (Aß) peptide has been studied in methanol. The peptide FFKLVFF is based on Aß(16-20) extended at the N terminus by two phenylalanine residues. The formation of amyloid-type fibrils is confirmed by Congo Red staining, thioflavin T fluorescence and circular dichroism experiments. FTIR points to the formation of ß-sheet structures in solution and in dried films and suggests that aggregation occurs at low concentration and is not strongly affected by further increase in concentration, i.e. the peptide is a strong fibril-former in methanol. UV fluorescence experiments on unstained peptide and CD point to the importance of aromatic interactions between phenylalanine groups in driving aggregation into ß-sheets. The CD spectrum differs from that usually observed for ß-sheet assemblies formed by larger peptides or proteins and this is discussed for solutions in methanol and also trifluoroethanol. The fibril structure is imaged by transmission electron microscopy and scanning electron microscopy on dried samples and is confirmed by small-angle X-ray scattering experiments in solution.

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