Using Proteomic Strategies for Sequencing and Post-Translational Modifications Assignment of Antigen-5, a Major Allergen from the Venom of the Social Wasp Polybia paulista

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

All-loop infrared-divergent behavior of most-subleading-color gauge-theory amplitudes

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Correspondence between the one-loop three-point vertex and the Y and Delta electric resistor networks

Different mathematical methods have been applied to obtain the analytic result for the massless triangle Feynman diagram yielding a sum of four linearly independent (LI) hypergeometric functions of two variables F-4. This result is not physically acceptable when it is embedded in higher loops, because all four hypergeometric functions in the triangle result have the same region of convergence and further integration means going outside those regions of convergence. We could go outside those regions by using the well-known analytic continuation formulas obeyed by the F-4, but there are at least two ways we can do this. Which is the correct one? Whichever continuation one uses, it reduces a number of F-4 from four to three. This reduction in the number of hypergeometric functions can be understood by taking into account the fundamental physical constraint imposed by the conservation of momenta flowing along the three legs of the diagram. With this, the number of overall LI functions that enter the most general solution must reduce accordingly. It remains to determine which set of three LI solutions needs to be taken. To determine the exact structure and content of the analytic solution for the three-point function that can be embedded in higher loops, we use the analogy that exists between Feynman diagrams and electric circuit networks, in which the electric current flowing in the network plays the role of the momentum flowing in the lines of a Feynman diagram. This analogy is employed to define exactly which three out of the four hypergeometric functions are relevant to the analytic solution for the Feynman diagram. The analogy is built based on the equivalence between electric resistance circuit networks of types Y and Delta in which flows a conserved current. The equivalence is established via the theorem of minimum energy dissipation within circuits having these structures.

The closed-string 3-loop amplitude and S-duality

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

Identification of two novel cytolysins from the hydrozoan Olindias sambaquiensis (Cnidaria)

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

Functional and Topological Studies with Trp-Containing Analogs of the Peptide StII(1-30) Derived From the N-Terminus of the Pore Forming Toxin Sticholysin II: Contribution to Understand its Orientation in Membrane

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Interaction of Organophosphorus Pesticides with DNA Nucleotides on a Boron-Doped Diamond Electrode

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

Selective DMSO-induced conformational changes in proteins from Raman optical activity

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

Lectinhistochemical staining of granuloma induced by bacillus Calmette- Guerin in Piaractus mesopotamicus

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

Investigation of DMSO-Induced Conformational Transitions in Human Serum Albumin Using Two-Dimensional Raman Optical Activity Spectroscopy

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

The effects of the C-terminal amidation of mastoparans on their biological actions and interactions with membrane-mimetic systems

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

Prospecção de novos peptídeos com ação leishmanicida por dinâmica molecular

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Estudo das interações entre proteína NS1 do hRSV e flavonóides utilizando métodos biofísicos

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

Novos peptídeos sintéticos e estudo da interação com membranas modelo: efeito de modificações no N-terminal na atividade lítica e antimicrobiana

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Ineraction Model Between HRSV G-Protein and Flavonoids

Background: Acute respiratory infections (ARI) are the leading cause of infant mortality in the world, and human respiratory syncytial virus (HRSV) is one of the main agents of ARI. One of the key targets of the adaptive host immune response is the RSV G-protein, which is responsible for attachment to the host cell. There is evidence that compounds such as flavonoids can inhibit viral infection in vitro. With this in mind, the main purpose of this study was to determine, using computational tools, the potential sites for interactions between G-protein and flavonoids. Results: Our study allowed the recognition of an hRSV G-protein model, as well as a model of the interaction with flavonoids. These models were composed, mainly, of -helix and random coil proteins. The docking process showed that molecular interactions are likely to occur. The flavonoid kaempferol-3-O-α-L-arabinopyranosil-(2 → 1)-α-L-apiofuranoside-7-O-α-L-rhamnopyranoside was selected as a candidate inhibitor. The main forces of the interaction were hydrophobic, hydrogen and electrostatic. Conclusions: The model of G-protein is consistent with literature expectations, since it was mostly composed of random coils (highly glycosylated sites) and -helices (lipid regions), which are common in transmembrane proteins. The docking analysis showed that flavonoids interact with G-protein in an important ectodomain region, addressing experimental studies to these sites. The determination of the G-protein structure is of great importance to elucidate the mechanism of viral infectivity, and the results obtained in this study will allow us to propose mechanisms of cellular recognition and to coordinate further experimental studies in order to discover effective inhibitors of attachment proteins.