8 resultados para Protein Charge

em Repositório Institucional UNESP - Universidade Estadual Paulista "Julio de Mesquita Filho"


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As vespas sociais são predadoras de várias espécies de insetos e, portanto, o estudo de suas presas pode revelar seu potencial para programas de controle biológico de pragas. Durante o período de setembro de 2000 a janeiro de 2002, foram realizadas 70h de coleta de presas capturadas em doze ninhos de Polybia platycephala Richards, localizados em áreas urbanas do município de Juiz de Fora, MG. As presas capturadas por P. platycephala compreenderam cinco ordens de insetos: Diptera (33,4%), Lepidoptera (28,6%), Hemiptera (12,0%), Hymenoptera (9,4%) e Coleoptera (7,2%). O peso médio da carga protéica transportada pelas vespas foi 1,9 ±1,6 mg (n = 34, 0,3 - 6,2 mg), e a taxa média de proteína transportada por dia foi 22,8 mg. de acordo com os resultados, pode-se estimar a captura de 4.380 presas por ano por uma única colônia de P. platycephala. Desta forma, a espécie pode ser utilizada em programas de manejo em ambientes urbanos contribuindo para o controle de insetos pragas como larvas de pernilongos, lagartas desfolhadoras de plantas de jardins, pulgões e formas aladas de formigas.

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

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In an attempt to optimize a high yield, high efficiency artificial photosynthetic protein we have discovered unique energy and spatial architecture limits which apply to all light-activated photosynthetic systems. We have generated an analytical solution for the time behavior of the core three cofactor charge separation element in photosynthesis, the photosynthetic cofactor triad, and explored the functional consequences of its makeup including its architecture, the reduction potentials of its components, and the absorption energy of the light absorbing primary-donor cofactor. Our primary findings are two: First, that a high efficiency, high yield triad will have an absorption frequency more than twice the reorganization energy of the first electron transfer, and second, that the relative distance of the acceptor and the donor from the primary-donor plays an important role in determining the yields, with the highest efficiency, highest yield architecture having the light absorbing cofactor closest to the acceptor. Surprisingly, despite the increased complexity found in natural solar energy conversion proteins, we find that the construction of this central triad in natural systems matches these predictions. Our analysis thus not only suggests explanations for some aspects of the makeup of natural photosynthetic systems, it also provides specific design criteria necessary to create high efficiency, high yield artificial protein-based triads.

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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C-reactive protein (CRP) is an acute phase protein whose levels are increased in many disorders. Levels greater than 3 mu g/mL serum have hitherto been considered to indicate pathology, but there is increasing interest in assessments between 0.1 and 10 mu g/mL, which have been found to correlate with severity of risk for cardiovascular disease. We report herein the generation of both antibody and Affimer based impedance immunoassays for CRP that are substantially more sensitive than clinically utilized immunonephelometry and immunoturbidity assessments. Significant in this study is not only the use of a constrained peptide to detect a clinically important target but also that derived electrochemical impedance assays can be highly sensitive even with probes whose relatively weak (mu M) affinities are not amenable to target detection by surface plasmon resonance (SPR). Key to this finding is acknowledging that receptive surfaces of comparatively low initial steric bulk and charge transfer resistance are especially primed to be highly responsive to target binding in electroanalytical assays of this type.

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C-reactive protein (CRP) is an acute phase protein whose levels are increased in many disorders. There exists, in particular, a great deal of interest in the correlation between blood serum levels and the severity of risk for cardiovascular disease. A sensitive, label-free, non-amplified and reusable electrochemical impedimetric biosensor for the detection of CRP in blood serum was developed herein based on controlled and coverage optimised antibody immobilization on standard polycrystalline gold electrodes. Charge transfer resistance changes were highly target specific, linear with log. CRP. concentration across a 0.5-50. nM range and associated with a limit of detection of 176. pM. Significantly, the detection limits are better than those of current CRP clinical methods and the assays are potentially cheap, relatively automated, reusable, multiplexed and highly portable. The generated interfaces were capable not only of comfortably quantifying CRP across a clinically relevant range of concentrations but also of doing this in whole blood serum with interfaces that were, subsequently, reusable. The importance of optimising receptor layer resistance in maximising assay sensitivity is also detailed. © 2012.