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1.
Int J Cosmet Sci ; 2019 Dec 18.
Artigo em Inglês | MEDLINE | ID: mdl-31850543

RESUMO

OBJECTIVE: To demonstrate that the tryptophan (Trp) fluorescence of natural white hair is much weaker than other unpigmented keratin fibres such as wool, cashmere, rabbit hair and mink fur, and to explore possible reasons for this behaviour. The origin of the blue visible fluorescence (~450 nm) excited by UVA radiation in the range 360-380 nm, often associated with Trp degradation products, is also discussed and compared to other fibrous and globular proteins. METHODS: As the fluorescence spectrum of keratin fibres usually contains at least two major features, a visual comparison is more effectively demonstrated by creating a 3D contour plot of excitation versus emission wavelength, which is sometimes referred to as an excitation emission matrix (EEM). RESULTS: The Trp fluorescence from white hair is very much weaker than for wool, cashmere, rabbit hair and mink fur, but its visible fluorescence emission is stronger. Oxidation and reduction have little effect on the Trp intensity, which suggests quenching by cystine is not a major factor. Decuticulation of hair fibres had no effect on the Trp intensity showing that the increased number of cuticle scales surrounding the fibre cortex is not responsible. Trp fluorescence is very sensitive to exposure to UVB wavelengths, so possibly its low intensity in hair is due to greater levels of environmental exposure to sunlight than the other fibres examined. CONCLUSION: Trp fluorescence from natural white hair is either extremely weak or completely absent, in contrast to the four other keratin fibres examined. It is possible that environmental exposure to UV wavelengths present in sunlight contributes to a reduction in the Trp fluorescence intensity of white hair. However another explanation is that Trp is quenched, by either an unknown substance introduced into hair during keratinisation, or as a result of regular exposure to personal care products, which may interact with Trp or tyrosine residues and disrupt the energy transfer process involved in keratin fluorescence. Further studies will be required to definitively determine the cause.

2.
Amino Acids ; 43(3): 1277-85, 2012 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-22218994

RESUMO

UV-visible diffuse reflectance (DR) spectra of the fibrous proteins wool and feather keratin, silk fibroin and bovine skin collagen are presented. Natural wool contains much higher levels of visible chromophores across the whole visible range (700-400 nm) than the other proteins and only those above 450 nm are effectively removed by bleaching. Both oxidative and reductive bleaching are inefficient for removing yellow chromophores (450-400 nm absorbers) from wool. The DR spectra of the four UV-absorbing amino acids tryptophan, tyrosine, cystine and phenylalanine were recorded as finely ground powders. In contrast to their UV-visible spectra in aqueous solution where tryptophan and tyrosine are the major UV absorbing species, surprisingly the disulphide chromophore of solid cystine has the strongest UV absorbance measured using the DR remission function F(R)(∞). The DR spectra of unpigmented feather and wool keratin appear to be dominated by cystine absorption near 290 nm, whereas silk fibroin appears similar to tyrosine. Because cystine has a flat reflectance spectrum in the visible region from 700 to 400 nm and the powder therefore appears white, cystine absorption does not contribute to the cream colour of wool despite the high concentration of cystine residues near the cuticle surface. The disulphide absorption of solid L: -cystine in the DR spectrum at 290 nm is significantly red shifted by ~40 nm relative to its wavelength in solution, whereas homocystine and lipoic acid showed smaller red shifts of 20 nm. The large red shift observed for cystine and the large difference in intensity of absorption in its UV-visible and DR spectra may be due to differences in the dihedral angle between the crystalline solid and the solvated molecules in solution.


Assuntos
Proteínas Aviárias/química , Colágenos Fibrilares/química , Fibroínas/química , Queratinas/química , Lã/química , Animais , Aves , Clareadores/química , Bovinos , Cisteína/química , Plumas/química , Homocisteína/química , Peróxido de Hidrogênio/química , Oxirredução , Ovinos , Espectrofotometria Ultravioleta
3.
Luminescence ; 27(5): 362-70, 2012.
Artigo em Inglês | MEDLINE | ID: mdl-23044771

RESUMO

Thermal luminescence (TL) spectra of polyamides were measured with a Fourier-transform chemiluminescence spectrometer to elucidate the emission mechanism. A TL band of ε-polylysine with a peak at 542 nm observed at 403 K was assigned to the emission due to the interaction of the -CO-NH- group with oxygen molecules by comparison with nylon-6, polyglycine, and polyalanine. When the sample was kept at 453 K, the intensity of the TL band decreased and the wavelength of the peak shifted to 602 nm, which was assigned to the emission due to the interaction of the NH2 group on the side chain with oxygen molecules by comparison with monomeric lysine. A weak emission with a peak at 668 nm was assigned to the advanced glycosylation end products (AGEs) yielded by the Maillard reaction with a catalytic amount of water. To understand this reaction and to examine the TL emission of AGEs, we measured TL spectra of mixtures of polylysine and reducing sugars such as glucose, maltose, lactose, and dextrin. The minimum temperature for TL emission, wavelength of the peak and the relative intensities of the TL emission were found to depend on the size of the sugars.


Assuntos
Produtos Finais de Glicação Avançada/química , Nylons/química , Temperatura Alta , Luminescência , Reação de Maillard , Estrutura Molecular , Oxirredução
4.
Amino Acids ; 38(5): 1395-405, 2010 May.
Artigo em Inglês | MEDLINE | ID: mdl-19763784

RESUMO

Chemiluminescence (CL) with maximum emission in the range 550-650 nm is observed when proteins and certain amino acids are heated in air, and CL intensity is significantly reduced in nitrogen. Of the 20 common amino acids, lysine (Lys) has the highest thermal CL intensity by a factor of approximately 30 over arginine, threonine and asparagine. This finding differs from previous studies on amino acids and proteins oxidised using free radical initiators or singlet oxygen, where tryptophan was the dominant factor for CL emission. CL from heating solid Lys in air is accompanied by browning and the generation of fluorescent products which are characteristic of advanced glycosylation end products (AGEs) in thermally treated milk proteins. During thermal oxidation, Lys may react with its own carbonyl oxidation products to form fluorescent compounds similar to AGEs via the formation of Schiff bases. The mechanism of thermal oxidation of proteins may be similar to polyamide polymers, where reaction of free primary amino groups with carbonyls to form Schiff bases plays a key role.


Assuntos
Aminoácidos/química , Luminescência , Proteínas/química , Temperatura , Produtos Finais de Glicação Avançada/química , Oxirredução , Espectrometria de Fluorescência
5.
Photochem Photobiol ; 84(1): 145-53, 2008.
Artigo em Inglês | MEDLINE | ID: mdl-18173714

RESUMO

The application of fluorescent whitening agents (FWAs) significantly accelerates the photoyellowing of wool and silk under exposure to the ultraviolet and visible components of sunlight <500 nm. The photochemistry involved in this process is poorly understood, particularly the role of photoproducts derived directly from the FWA itself. Hydroxylation was identified as the key initial mechanism of photodegradation leading to coloration of the solution in the irradiation of the stilbene-derived FWA 4,4'-bis(2-sulfostyryl)biphenyl (DSBP) in the presence of hydrogen peroxide (H2O2). Polyhydroxylated DSBP derivatives were implicated as critical intermediates in the formation of yellow photoproducts under these conditions. The formation of trace quantities of DSBP quinone derivatives subsequent to hydroxylation was identified as the key cause of DSBP photoyellowing. These results are the first successful characterization of yellow photoproducts resulting directly from irradiation of a stilbene-based FWA. Formation of these yellow stilbene-based FWA-derived photoproducts may occur on the surface of FWA-treated wool exposed to simulated sunlight, as previous work has shown that H2O2 is photogenerated when wet FWA-treated wool is exposed to light. These results therefore suggest that yellow FWA-derived photoproducts contribute to the accelerated photoyellowing of FWA-treated wool.


Assuntos
Compostos de Bifenilo/química , Corantes Fluorescentes/química , Estilbenos/química , Cor , Estrutura Molecular , Oxirredução , Fotoquímica , Espectrometria de Massas por Ionização por Electrospray , Espectrometria de Massas em Tandem
6.
J Photochem Photobiol B ; 92(3): 135-43, 2008 Sep 18.
Artigo em Inglês | MEDLINE | ID: mdl-18617417

RESUMO

The wool fibre has a complex morphology, consisting of an outer layer of cuticle scales surrounding an inner cortex. These two components are hard to separate effectively except by using harsh chemical treatments, making it difficult to determine the susceptibility of the different components of the fibre to photoyellowing. An approach to this problem based on mechanical fibre modification is described. To expose the inner cortex of wool to different degrees, clean wool fibres were converted into 'powders' of various fineness via mechanical chopping, air-jet milling, ball milling or their combination. Four types of powdered wool (samples A, B, C and D) were produced with reducing particle size distributions and an increasing level of surface damage as observed using SEM. Sample A contained essentially intact short fibre snippets and sample D contained a large amount of exposed cortical materials. Samples B and C contained a mixture of short fibre snippets and cortical materials. Solid wool discs were then compressed from the corresponding powder samples in a polished stainless steel die to enable colour measurement and UV irradiation studies. ATR-FTIR studies on powder discs demonstrated a small shift in the amide I band from 1644cm(-1) for disc A to 1654cm(-1) for disc D due to the different structures of the wool cuticle and cortex, in agreement with previous studies. Similarly an increase in the intensity ratio of the amide I to amide II band (1540cm(-1)) was observed for disc D, which contains a higher fraction of cortical material at the surface of the disc. Discs prepared from sample D appeared the lightest in colour before exposure and had the slowest photoyellowing rate, whereas discs made from powders A-C with a higher level of cuticle coverage were more yellow before exposure and experienced a faster rate of photoyellowing. This suggests that the yellow chromophores of wool may be more prevalent in cuticle scales, and that wool photoyellowing occurs to a greater extent in the cuticle than in the cortex. Photo-induced chemiluminescence measurements showed that sample D had a higher chemiluminescence intensity after exposure to UVA radiation and a faster decay rate than samples A and B. Thus one of the roles of the wool cuticle may be to protect the cortex by quenching of free radical oxidation during exposure to the UV wavelengths present in sunlight.


Assuntos
Proteínas/efeitos da radiação , Lã/efeitos da radiação , Animais , Cor , Luminescência , Microscopia Eletrônica de Varredura , Tamanho da Partícula , Fotoquímica , Proteínas/química , Proteínas/ultraestrutura , Ovinos , Espectroscopia de Infravermelho com Transformada de Fourier , Raios Ultravioleta , Lã/química , Lã/ultraestrutura
7.
J Photochem Photobiol B ; 133: 27-38, 2014 Apr 05.
Artigo em Inglês | MEDLINE | ID: mdl-24667184

RESUMO

One of the current concerns with the application of nanoparticles in sunscreens, and in particular nano-TiO2 and ZnO, is their potential to photogenerate free radicals and reactive oxygen species (ROS) when they absorb ultraviolet wavelengths from sunlight. Free radicals and ROS are known to be associated with UV-induced skin damage and oxidative stress, from which sunscreens are expected to offer significant protection. Here we describe a simple method, based on chemiluminescence emission, for detecting free radicals generated in commercial sunscreens alone, and when applied to various substrates, following exposure to UVA (320-400nm) radiation. This photo-induced chemiluminescence (PICL) technique could be used to optimise sunscreen formulations so as to minimise free radical photogeneration during exposure to sunlight.


Assuntos
Radicais Livres/análise , Medições Luminescentes , Protetores Solares/química , Raios Ultravioleta , Animais , Catálise , Feminino , Nanopartículas Metálicas/química , Nanopartículas Metálicas/toxicidade , Camundongos , Camundongos Pelados , Rodaminas/química , Rodaminas/metabolismo , Pele/efeitos dos fármacos , Pele/efeitos da radiação , Protetores Solares/farmacologia , Titânio/química , Óxido de Zinco/química
8.
J Photochem Photobiol B ; 114: 140-6, 2012 Sep 03.
Artigo em Inglês | MEDLINE | ID: mdl-22727928

RESUMO

Several previous studies have reported luminescence emission from skin following exposure to UVA radiation in air. We show that UVA irradiation of biomaterials and polymers in oxygen, including bovine stratum corneum, followed by photon counting results in a complex emission due to a combination of photophysical processes together with photo-induced chemiluminescence (PICL). The photophysical processes include fluorescence, phosphorescence and charge-recombination luminescence. By irradiating materials in an inert atmosphere such as nitrogen and allowing photophysical light emission to fully decay before admitting oxygen, the weak photo-induced chemiluminescence generated via free radical reactions with oxygen can be separated and analysed. PICL emission from bovine stratum corneum is weaker than for wool keratin and bovine skin collagen, probably due to its higher water content, and the presence of the natural antioxidants ascorbate and tocopherol.


Assuntos
Pele/efeitos da radiação , Raios Ultravioleta , Animais , Antioxidantes/química , Antioxidantes/metabolismo , Ácido Ascórbico/química , Ácido Ascórbico/metabolismo , Bovinos , Medições Luminescentes , Oxigênio/química , Oxigênio/metabolismo , Vitamina E/química , Vitamina E/metabolismo
9.
J Photochem Photobiol B ; 98(2): 118-27, 2010 Feb 12.
Artigo em Inglês | MEDLINE | ID: mdl-20042345

RESUMO

Photo-oxidation of proteinaceous fibres correlates directly to lowered appearance retention and performance, with particular commercial significance for wool and human hair. We here outline the first detailed proteomic evaluation of differential photo-oxidation occurring in the cuticle and cortex of wool fibres. After exposure of whole wool to UVB irradiation, physical disruption techniques designed to minimise further oxidative modification were utilised to prepare enriched cuticle and cortex fractions. This was followed by comprehensive redox proteomic analyses of photo-oxidation via the location within the fibre components of modifications to aromatic residues. An oxidative classification system was developed and applied to provide further insight into differential photo-oxidation. These results were compared with coloration changes observed within the cuticular and cortical components of the fibre. In this study, although the cuticle was observed to have a higher level of baseline oxidation, the cortex exhibited significantly higher levels of photo-oxidation under UVB irradiation. These proteomic results were supported by the observation of significantly higher photoyellowing within the cortex than within the cuticle. It has been assumed that fibre photo-oxidation was predominantly confined to the wool cuticle, and that changes within the cuticle had the greatest effect on appearance retention. These results provide new insight into the contribution of the cortex to photo-induced discoloration of proteinaceous animal fibres.


Assuntos
Proteômica , Raios Ultravioleta , Lã/metabolismo , Sequência de Aminoácidos , Animais , Queratinas/química , Dados de Sequência Molecular , Oxirredução , Peptídeos/análise , Peptídeos/química , Lã/química , Lã/efeitos da radiação
10.
Photochem Photobiol ; 85(6): 1314-21, 2009.
Artigo em Inglês | MEDLINE | ID: mdl-19709380

RESUMO

Fibrous proteins discolor on exposure to the UV component of sunlight. This effect is exacerbated in the presence of fluorescent whitening agents (FWAs), which are often applied to textiles to improve product brightness. Tryptophan photoproducts have been identified as significant contributors to protein photoyellowing; however, the role of non-tryptophan-derived chromophores is less clear. In this study bovine collagen, containing no tryptophan residues, was irradiated in the presence and absence of the stilbene-derived FWA, 4,4'-bis(2-sulfostyryl)biphenyl (DSBP) and photoproducts were identified using mass spectrometry. Photoyellowing was found to be dependent on the presence of the FWA, attributed to amplified generation of reactive oxygen species (ROS), particularly hydroxyl radicals and peroxynitrite. Four key proteinaceous photomodifications contributing directly to photoyellowing were located in irradiated collagen pretreated with DSBP, namely dopa, nitrophenylalanine, nitrotyrosine and nitrohistidine. This represents the first direct characterization of the three nitrated residues in the photoyellowing of an isolated fibrous protein, and implicates the ROS, peroxynitrite, as a key contributor to protein photoyellowing. Direct oxidative modification of the FWA itself was also observed. This study demonstrates that, even in the absence of tryptophan residues, significant photomodification of protein residues leading to chromophore formation occurs in the presence of an FWA.


Assuntos
Compostos de Bifenilo/química , Colágeno/química , Fotoquímica , Estilbenos/química , Sequência de Aminoácidos , Animais , Compostos de Bifenilo/farmacologia , Bovinos , Cromatografia Líquida , Colágeno/classificação , Colágeno/efeitos dos fármacos , Cor , Corantes/química , Corantes/farmacologia , Corantes Fluorescentes/metabolismo , Espectrometria de Massas , Dados de Sequência Molecular , Estilbenos/farmacologia
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