8 resultados para small molecule libraries
em Repositório Institucional UNESP - Universidade Estadual Paulista "Julio de Mesquita Filho"
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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In this paper, we report the development of a sensitive label-free impedimetric biosensor based on the use of affibody as bioreceptor and gold nanostructured screen-printed graphite as a sensor platform for the detection of human epidermal growth factor receptor 2 (HER2). The affisensor is realized by immobilizing a terminal cysteine-modified affibody on gold nanoparticles. The sensor was characterized by electrochemical techniques and scanning electron microscopy (SEM). Furthermore, surface plasmon resonance (SPR) technology was also applied to explore the potential of affibodies as small-molecule discriminating tools. Using optimized experimental conditions, a single-use affisensor showed a good analytical performance for HER2 detection from 0 to 40μg/L. The estimated limit of detection was 6.0μg/L. Finally, the realized affisensor was applied to human serum samples.
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The mast cell tumor (MCT) is the second most common type of tumor in dogs. It is characterized by uncontrolled proliferation of mast cells in the skin. Treatment involves surgical resection, chemotherapy and radiotherapy. Recently, new treatment protocols have been developed, such as the use of tyrosine kinase inhibitors. With the increasing knowledge about the genome and the evolution of methods in molecular genetics, drugs with specific molecular targets are surely going to become promising therapeutic modalities in the near future. Besides being involved in the normal cell cycle, some studies suggest that tyrosine kinases have a fundamental role in neoplastic processes. Therefore, some strategies such as the development of antibodies anti-receptors for tyrosine kinases and small-molecule tyrosine kinase receptor inhibitors have been developed in an attempt to inhibit tumor development. The purpose of this review is to describe the use of tyrosine kinase inhibitors in the treatment of mast cell tumors in dogs.
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
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The carbonyl complexes [WCl(CO)(3)(bipy) (HgCl)] (1), [Fe(CO)(4)(HgCl)(2)] (2) and W(CO)(6)] (3) were immobilized on a silica gel surface organofunctionalized with piperazine groups. The products obtained were studied by IR spectroscopy and small angle X-ray scattering (SAXS) techniques. The IR data show that the immobilization of heterobimetallic compounds 1 and 2, on the functionalized surface, occurred through the mercury atom, while for 3 the displacement of one CO group by the nitrogen of a piperazine molecule was observed. The data obtained from SAXS indicate that particles have a uniform size and reveal suitable modifications on the functionalized surface after immobilization of metal carbonyl complexes. The average intermolecular distance (l(ij)) for piperazine ligands on support is 8.7 Angstrom, for the metal carbonyl complex 1 it is 18.8 Angstrom, for complex 2 it is 16.2 Angstrom and for complex 3 it is 15.3 Angstrom. Copyright (C) 1996 Elsevier B.V. Ltd
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The spin label TEMPO does not show a binding to myoglobin molecule in solution. This is probably due to the fact that this protein does not have a hydrophobic pocket large enough to accommodate the TEMPO molecule. In the crystal the spin label is bound and two kinds of spectra are observed: one isotropic and the other anisotropic. The anisotropic site is probably an intermolecular one. The correlation time for the label in the crystal is very sensitive to temperature showing a transition near 30 °C. This change can be explained as a result of the conformational change observed for myoglobin near this temperature: the motion of the spin label becomes more restricted below this temperature. Change in hydration is the probable cause of this structural change. The changes in the EPR spectra of the anisotropic label suggest that it is bound near the first layers of protein in the crystal. © 1985 Societá Italiana di Fisica.
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Axillary bud outgrowth determines shoot architecture and is under the control of endogenous hormones and a fine-tuned gene-expression network, which probably includes small RNAs (sRNAs). Although it is well known that sRNAs act broadly in plant development, our understanding about their roles in vegetative bud outgrowth remains limited. Moreover, the expression profiles of microRNAs (miRNAs) and their targets within axillary buds are largely unknown. Here, we employed sRNA next-generation sequencing as well as computational and gene-expression analysis to identify and quantify sRNAs and their targets in vegetative axillary buds of the biofuel crop sugarcane (Saccharum spp.). Computational analysis allowed the identification of 26 conserved miRNA families and two putative novel miRNAs, as well as a number of trans-acting small interfering RNAs. sRNAs associated with transposable elements and protein-encoding genes were similarly represented in both inactive and developing bud libraries. Conversely, sequencing and quantitative reverse transcription-PCR results revealed that specific miRNAs were differentially expressed in developing buds, and some correlated negatively with the expression of their targets at specific stages of axillary bud development. For instance, the expression patterns of miR159 and its target GAMYB suggested that they may play roles in regulating abscisic acid-signalling pathways during sugarcane bud outgrowth. Our work reveals, for the first time, differences in the composition and expression profiles of diverse sRNAs and targets between inactive and developing vegetative buds that, together with the endogenous balance of specific hormones, may be important in regulating axillary bud outgrowth. © 2013 © The Author(2) [2013].
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Small-angle X-ray scattering (SAXS) was used to study structural characteristics of human serum albumin (HSA) in solution under different pH conditions. Guinier analysis of SAXS results yielded values of the molecular radius of gyration ranging from 26.7 Å to 34.5 Å for pH varying from 2.5 to 7.0. This suggests the existence of significant differences in the overall shape of the molecule at different pH. Molecular models based on subdomains with different spatial configurations were proposed. The distance distribution functions associated with these models were calculated and compared with those determined from the experimental SAXS intensity functions. The conclusion of this SAXS study is that the arrangement of molecular subdomains is clearly pH dependent; the molecule adopting more or less compact configuration for different pH conditions. The conclusions of this systematic study on the modification in molecular shape of HSA as a response to pH changes is consistent with those of previous investigations performed for particular pH conditions.