Jocley Q Araújo

Publications (2)3.13 Total impact

• Article: CoMFA/CoMSIA 3D-QSAR of pyrimidine inhibitors of Pneumocystis carinii dihydrofolate reductase.

  Osvaldo A Santos-Filho, Delphine Forge, Lucas V B Hoelz, Guilherme B L de Freitas, Thiago O Marinho, Jocley Q Araújo, Magaly G Albuquerque, Ricardo B de Alencastro, Nubia Boechat
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  ABSTRACT: Pneumocystis carinii is typically a non-pathogenic fungus found in the respiratory tract of healthy humans. However, it may cause P. carinii pneumonia (PCP) in people with immune deficiency, affecting mainly premature babies, cancer patients and transplant recipients, and people with acquired immunodeficiency syndrome (AIDS). In the latter group, PCP occurs in approximately 80% of patients, a major cause of death. Currently, there are many available therapies to treat PCP patients, including P. carinii dihydrofolate reductase (PcDHFR) inhibitors, such as trimetrexate (TMX), piritrexim (PTX), trimethoprim (TMP), and pyrimethamine (PMT). Nevertheless, the high percentage of adverse side effects and the limited therapeutic success of the current drug therapy justify the search for new drugs rationally planned against PCP. This work focuses on the study of pyrimidine inhibitors of PcDHFR, using both CoMFA and CoMSIA 3D-QSAR methods.
  Journal of Molecular Modeling 04/2012; 18(9):4061-72. · 1.80 Impact Factor
• Article: Dynamical behaviour of the human β1-adrenoceptor under agonist binding

  Lucas V.B. Hoelz, Rafael C. Bernardi, Bruno A.C. Horta, Jocley Q. Araújo, Magaly G. Albuquerque, Joaquim F.M. da Silva, Pedro G. Pascutti, Ricardo B. de Alencastro
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  ABSTRACT: The human β1-adrenoceptor (hβ1AR) is a transmembrane (TM) protein responsible for the signal transduction pathway via agonist interaction. Despite its importance, hβ1AR activation mechanism is still unclear. The most studied and widely accepted mechanism is the disruption of a salt bridge between TM3 arginine and TM6 glutamic acid, called ionic lock. In this work, we constructed a functional hβ1AR-model equilibrated in a membrane environment to study the influence of agonist binding on the dynamical behaviour of hβ1AR and on the opening of the ionic lock. The results indicate that the agonist (R-noradrenaline) disturbs the hβ1AR, causing a TM helices rotation, disrupting the ionic lock. This rotational motion occurs in opposite directions in the intercellular and extracellular domains of hβ1AR, opening the ionic lock.
  Molecular Simulation 09/2011; 37(11):907-913. · 1.33 Impact Factor