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1.
J Biomol Struct Dyn ; 41(2): 753-763, 2023 02.
Artigo em Inglês | MEDLINE | ID: mdl-34871148

RESUMO

Body's homeostasis is dependent on many factors, such as maintaining balance between free radicals formation and degradation. Human serum albumin (HSA) also plays an important role in homeostasis. The aim of this study was thermodynamic analysis of the interaction between ketoprofen (KET), naproxen (NPX), diclofenac (DIC) and HSA, as well as the effect of drug-albumin binding on HSA antioxidant activity using calorimetric and spectrophotometric techniques. Based on the calorimetric analysis it has been shown that accompanied by hydrophobic interaction drugs-albumin binding is an exoenergetic reaction. All analyzed drugs and HSA showed the ability to react with free radicals such as a radical cation, formed as a result of the reaction between 2,2'-Azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) and potassium persulfate (K2S2O8). Using ABTS assay a synergistic effect of ketoprofen (KET) and naproxen (NPX) on HSA antioxidant activity was observed while the effect of diclofenac (DIC) binding with albumin was probably additive. Because some medications including KET, NPX and DIC belong to over the counter (OTC) non-steroidal anti-inflammatory drugs (NSAIDs), it is necessary to understand their influence on HSA antioxidant activity.Communicated by Ramaswamy H. Sarma.


Assuntos
Cetoprofeno , Humanos , Cetoprofeno/química , Naproxeno/farmacologia , Naproxeno/química , Naproxeno/metabolismo , Antioxidantes/farmacologia , Albumina Sérica Humana , Diclofenaco/farmacologia , Diclofenaco/química , Albumina Sérica/química , Anti-Inflamatórios não Esteroides/química , Sítios de Ligação
2.
Nanotechnology ; 28(8): 085302, 2017 Feb 24.
Artigo em Inglês | MEDLINE | ID: mdl-28045378

RESUMO

We have studied the transition between two different magnetization reversal mechanisms for thin Co/Pd multilayers with perpendicular magnetic anisotropy, appearing in magnetic dot and antidot arrays, which were prepared by nanosphere lithography. Various ordered arrays of nanostuctures, both magnetic dots and antidots, were created by varying size and distance between the nanospheres employing RF-plasma etching. We have shown that the coercivity values reach a maximum for the array of antidots with a separation length close to the domain wall width. In this case, each area between three adjacent holes corresponds to a single domain configuration, which can be switched individually. On the contrary, small hole sizes and large volume of material between them results in domain wall propagation throughout the system accompanied by strong domain wall pinning at the holes. We have also shown the impact of edge effects on the magnetic anisotropy energy.

3.
Artigo em Inglês | MEDLINE | ID: mdl-26433342

RESUMO

The modification of human serum albumin (HSA) structure by non-enzymatic glycation is one of the underlying factors that contribute to the development of complications of diabetes and neurodegenerative diseases. The aim of the present work was to estimate how glycation of HSA altered its tertiary structure. Changes of albumin conformation were investigated by comparison of glycated (gHSA) and non-glycated human serum albumin (HSA) absorption spectra, red edge excitation shift (REES) and synchronous spectra. Effect of glycation on human serum albumin tertiary structure was also investigated by (1)H NMR spectroscopy. Formation of gHSA Advanced Glycation End-products (AGEs) caused absorption of UV-VIS light between 310 nm and 400 nm while for non-glycated HSA in this region no absorbance has been registered. Analysis of red edge excitation shift effect allowed for observation of structural changes of gHSA in the hydrophobic pocket containing the tryptophanyl residue. Moreover changes in the microenvironment of tryptophanyl and tyrosyl residues brought about AGEs on the basis of synchronous fluorescence spectroscopy have been confirmed. The influence of glycation process on serum albumin binding to 5-dimethylaminonaphthalene-1-sulfonamide (DNSA), 2-(p-toluidino) naphthalene-6-sulfonic acid (TNS), has been studied. Fluorescence analysis showed that environment of both binding site I and II is modified by galactose glycation.


Assuntos
Albumina Sérica/química , Compostos de Dansil/metabolismo , Glicosilação , Humanos , Interações Hidrofóbicas e Hidrofílicas , Naftalenossulfonatos/metabolismo , Estrutura Terciária de Proteína , Espectroscopia de Prótons por Ressonância Magnética , Albumina Sérica/metabolismo , Espectrometria de Fluorescência
4.
Spectrochim Acta A Mol Biomol Spectrosc ; 152: 645-53, 2016 Jan 05.
Artigo em Inglês | MEDLINE | ID: mdl-25735846

RESUMO

Human serum albumin (HSA), transporting protein, is exposed during its life to numerous factors that cause its functions become impaired. One of the basic factors --glycation of HSA--occurs in diabetes and may affect HSA-drug binding. Accumulation of advanced glycation end-products (AGEs) leads to diseases e.g. diabetic and non-diabetic cardiovascular diseases, Alzheimer disease, renal disfunction and in normal aging. The aim of the present work was to estimate how non-enzymatic glycation of human serum albumin altered its tertiary structure using fluorescence technique. We compared glycated human serum albumin by glucose (gHSA(GLC)) with HSA glycated by fructose (gHSA(FRC)). We focused on presenting the differences between gHSA(FRC) and nonglycated (HSA) albumin used acrylamide (Ac), potassium iodide (KI) and 2-(p-toluidino)naphthalene-6-sulfonic acid (TNS). Changes of the microenvironment around the tryptophan residue (Trp-214) of non-glycated and glycated proteins was investigated by the red-edge excitation shift method. Effect of glycation on ligand binding was examined by the binding of phenylbutazone (PHB) and ketoprofen (KP), which a primary high affinity binding site in serum albumin is subdomain IIA and IIIA, respectively. At an excitation and an emission wavelength of λex 335nm and λem 420nm, respectively the increase of fluorescence intensity and the blue-shift of maximum fluorescence was observed. It indicates that the glycation products decreases the polarity microenvironment around the fluorophores. Analysis of red-edge excitation shift method showed that the red-shift for gHSA(FRC) is higher than for HSA. Non-enzymatic glycation also caused, that the Trp residue of gHSA(FRC) becomes less accessible for the negatively charged quencher (I(-)), KSV value is smaller for gHSA(FRC) than for HSA. TNS fluorescent measurement demonstrated the decrease of hydrophobicity in the glycated albumin. KSV constants for gHSA-PHB systems are higher than for the unmodified serum albumin, while KSV values for gHSA-KP systems are only slightly lower than that obtained for HSA-KP. The affinity of PHB to the glycated HSA is stronger than to the non-glycated in the first class binding sites within subdomain IIA, in the vicinity of Trp-214. Ketoprofen bound to unmodified human serum albumin stronger than for glycated albumin and one class of binding sites is observed (Scatchard linear plots).


Assuntos
Albumina Sérica/química , Albumina Sérica/metabolismo , Anti-Inflamatórios não Esteroides/metabolismo , Corantes Fluorescentes/química , Produtos Finais de Glicação Avançada/análise , Produtos Finais de Glicação Avançada/metabolismo , Glicosilação , Humanos , Cetoprofeno/metabolismo , Modelos Moleculares , Naftalenossulfonatos/química , Fenilbutazona/metabolismo , Proibitinas , Estrutura Terciária de Proteína , Espectrometria de Fluorescência , Albumina Sérica Glicada
5.
Nanotechnology ; 23(10): 105703, 2012 Mar 16.
Artigo em Inglês | MEDLINE | ID: mdl-22361492

RESUMO

Scanning transmission x-ray microscopy (STXM) and magnetoresistance (MR) measurements are used to investigate the magnetic behavior of a nanoconstriction joining two micrometric electrodes (a pad and a wire). The reversal of the magnetization under variable external static magnetic fields is imaged. By means of a detailed analysis of the STXM images at the nanocontact area, the MR is calculated, based on diffusive anisotropic-MR. This MR agrees well with that obtained from electrical transport measurements, allowing a direct correlation between the MR signal and the magnetic reversal of the system. The magnetization behavior depends on the sample thickness and constriction dimensions. In 40 nm-thick samples, with 20 × 175 nm(2) contact areas, the magnetization at the two sides of the constriction forms a net angle of 90°, with a progressive evolution of the magnetization structure between the electrodes during switching. The MR in those cases has a more peaked shape than with 20 nm-thick electrodes and 10 × 80 nm(2) contact areas, where the magnetization forms 180° between them, with a wide domain wall pinned at the constriction. As a consequence of this configuration, a plateau in the MR is observed for about 20 Oe.

6.
Nanotechnology ; 20(47): 475704, 2009 Nov 25.
Artigo em Inglês | MEDLINE | ID: mdl-19858555

RESUMO

We systematically study individual micro- and nanometric polycrystalline cobalt wires grown by focused-electron-beam-induced-deposition. The deposits were grown in a range of aspect ratios varying from 1 up to 26. The minimum lateral dimension of the nanowires was 150 nm, for a thickness of 40 nm. Atomic force microscopy images show beam-current-dependent profiles, associated with different regimes of deposition. The magnetization reversal of individual nanowires is studied by means of the spatially resolved magneto-optical Kerr effect. Abrupt switching is observed, with a systematic dependence on the wire's dimensions. This dependence of the coercive field is understood in magnetostatic terms, and agrees well with previous results on cobalt wires grown with different techniques. The influence of compositional gradients along the structural profile on the magnetic reversal is studied by using micromagnetic simulations. This work demonstrates the feasibility of using this technique to fabricate highly pure magnetic nanostructures, and highlights the advantages and disadvantages of the technique with respect to more conventional ones.

7.
Folia Morphol (Warsz) ; 66(1): 62-8, 2007 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-17533596

RESUMO

This study analyses, using selected somatometric features, secular trend changes which have occurred over a quarter of a century in female and male students of the Medical University of Lódz. The study is based on the results of an anthropometric survey carried out among first-year students who commenced their studies in the academic years 1978/79 (240 females and 193 males), 1982/83 (347 females and 188 males), 1988/89 (178 females and 165 males) and 2003/04 (188 females and 77 males). The following features were examined in all participants in the survey: body height (B-v), the height of the lower body segment measured from a floor base to the crista iliaca at the point on the mid-axillary line (B-ic), shoulder width (a-a), intertrochanteric distance (tro-tro) and resting chest circumference. To compare average values Student's t-test was used with assumptions of equal and unequal variances. To gauge the magnitude of changes in specific features in the course of a quarter of a century a percentage difference in results was calculated for the years 2003/2004 and 1978/1979. The basis for the calculations was the initial value of a feature at the beginning of the period analysed. It was determined that in the 25-year period analysed (1978-2003) the young people commencing studies at the Medical University of Lódz exhibited an acceleration in the height of the lower body segment (B-ic) and of the intertrochanteric distance (tro-tro) and a deceleration in resting chest circumference. Additionally, an increase in shoulder width has been noted in female students; no significant intergenerational changes were noted in body height, although the last 15 years display certain symptoms of deceleration; there is an emerging tendency towards a blurring of the differences in body proportions between the sexes in the environment of the young people studying at the Medical University of Lódz.


Assuntos
Tamanho Corporal/fisiologia , Crescimento e Desenvolvimento/fisiologia , Estudantes de Medicina , Adulto , Antropometria , Estatura/fisiologia , Feminino , Humanos , Estudos Longitudinais , Masculino , Polônia , Caracteres Sexuais , Ombro/anatomia & histologia , Fatores Socioeconômicos , Tórax/anatomia & histologia
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