Institute for Scientific Research and Technology Services INDICASAT AIP

Panama

Institute for Scientific Research and Technology Services INDICASAT AIP

Panama
SEARCH FILTERS
Time filter
Source Type

Berrocal R.,Institute for Scientific Research and Technology Services INDICASAT AIP | Berrocal R.,Acharya Nagarjuna University | Vasquez V.,Institute for Scientific Research and Technology Services INDICASAT AIP | Vasquez V.,Acharya Nagarjuna University | And 4 more authors.
Molecular Neurobiology | Year: 2015

α-Synuclein, an abundant and conserved presynaptic brain protein, is implicated as a critical factor in Parkinson’s disease (PD). The aggregation of α-synuclein is believed to be a critical event in the disease process. α-Synuclein is characterized by a remarkable conformational plasticity, adopting different conformations depending on the environment. Therefore, it is classified as an “intrinsically disordered protein.” Recently, a debate has challenged the view on the intrinsically disordered behavior of α-synuclein in the cell. It has been proposed that α-synuclein is a stable tetramer with a low propensity for aggregation; however, its destabilization leads to protein misfolding and its aggregation kinetics. In our critical analysis, we discussed about major issues: (i) why α-synuclein conformational behavior does not fit into the normal secondary structural characteristics of proteins, (ii) potential amino acids involved in the complexity of misfolding in α-synuclein that leads to aggregation, and (iii) the role of metals in misfolding and aggregation. To evaluate the above critical issues, we developed bioinformatics models related to secondary and tertiary conformations, Ramachandran plot, free energy change, intrinsic disordered prediction, solvent accessibility, and FoldIndex pattern. To the best of our knowledge, this is a novel critical assessment to understand the misfolding biology of synuclein and its relevance to Parkinson’s disease. © 2014, Springer Science+Business Media New York.


Murillo E.,University of Panamá | Britton G.B.,Institute for Scientific Research and Technology Services INDICASAT AIP | Durant A.A.,University of Panamá | Durant A.A.,Institute for Scientific Research and Technology Services INDICASAT AIP
Journal of Pharmacy and Bioallied Sciences | Year: 2012

Objectives: The present research was undertaken to determine the antioxidant activity and total polyphenol content of cultivated and wild edible fruits consumed in Panama. Materials and Methods: 39 cultivated and wild edible fruits antioxidant activity and total polyphenol content was assessed by using the DPPH and the Folin-Ciocalteu assays, respectively. Results and Discussion: The antioxidant composition of the fruits varied between 1083.33 and 16.22 mg TEAC/100 g fresh weight. On the other hand, the total phenolic content of the 39 fruits tested ranged from 604.80 to 35.10 mg GAE/100 g FW. Ziziphus mauritania presented the highest antioxidant activity and the largest phenolic content, whereas most fruits had a moderate TEAC value. Conclusion: Fruits polyphenol content was strongly correlated with antioxidant properties, which pointed out the important role of these compounds in the prevention of many types of cancer, neurological ailments, and cardiovascular diseases through diverse antioxidant mechanisms.


Rao K.S.J.,Institute for Scientific Research and Technology Services INDICASAT AIP | Gupta V.B.,Edith Cowan University | Monica F.S.,Institute for Scientific Research and Technology Services INDICASAT AIP | Berrocal R.,Institute for Scientific Research and Technology Services INDICASAT AIP | Rao K.S.,University of Hyderabad
Journal of Alzheimer's Disease | Year: 2013

Amyloid-β peptide is presumably a key etiological factor involved in the pathogenesis of Alzheimer's disease (AD), and several hypotheses exist on the possible ways Aβ contributes to the progression of the disease. There are reports on the nuclear localization of Aβ and very limited evidence on its DNA binding property. The present study provided the mechanism of Aβ enantiomers binding to DNA and showed that Aβ40L induces ψ-DNA, while Aβ40D causes only altered B-DNA. Further, we evidenced the DNA nicking property of Aβ enantiomers and endonuclease mimicking behavior. The role of Aβ in modulating DNA stability was reported by altered melting temperature and ethidium bromide binding studies. The data provides new evidence on stereospecific dependent Aβ-DNA interaction and we discuss its biological relevance to neurodegeneration. Our results imply that Aβ-DNA interaction needs to be considered as a significant cause of the toxicity in the pathogenesis of AD. © 2013 - IOS Press and the authors. All rights reserved.


De La Guardia C.,Institute for Scientific Research and Technology Services INDICASAT AIP | De La Guardia C.,Acharya Nagarjuna University | Lleonart R.,Institute for Scientific Research and Technology Services INDICASAT AIP
BioMed Research International | Year: 2014

Dengue fever, a reemerging disease, is putting nearly 2. 5 billion people at risk worldwide. The number of infections and the geographic extension of dengue fever infection have increased in the past decade. The disease is caused by the dengue virus, a flavivirus that uses mosquitos Aedes sp. as vectors. The disease has several clinical manifestations, from the mild cold-like illness to the more serious hemorrhagic dengue fever and dengue shock syndrome. Currently, there is no approved drug for the treatment of dengue disease or an effective vaccine to fight the virus. Therefore, the search for antivirals against dengue virus is an active field of research. As new possible receptors and biological pathways of the virus biology are discovered, new strategies are being undertaken to identify possible antiviral molecules. Several groups of researchers have targeted the initial step in the infection as a potential approach to interfere with the virus. The viral entry process is mediated by viral proteins and cellular receptor molecules that end up in the endocytosis of the virion, the fusion of both membranes, and the release of viral RNA in the cytoplasm. This review provides an overview of the targets and progress that has been made in the quest for dengue virus entry inhibitors. © 2014 Carolina De La Guardia and Ricardo Lleonart.


PubMed | Acharya Nagarjuna University and Institute for Scientific Research and Technology Services INDICASAT AIP
Type: | Journal: BioMed research international | Year: 2014

Dengue fever, a reemerging disease, is putting nearly 2.5 billion people at risk worldwide. The number of infections and the geographic extension of dengue fever infection have increased in the past decade. The disease is caused by the dengue virus, a flavivirus that uses mosquitos Aedes sp. as vectors. The disease has several clinical manifestations, from the mild cold-like illness to the more serious hemorrhagic dengue fever and dengue shock syndrome. Currently, there is no approved drug for the treatment of dengue disease or an effective vaccine to fight the virus. Therefore, the search for antivirals against dengue virus is an active field of research. As new possible receptors and biological pathways of the virus biology are discovered, new strategies are being undertaken to identify possible antiviral molecules. Several groups of researchers have targeted the initial step in the infection as a potential approach to interfere with the virus. The viral entry process is mediated by viral proteins and cellular receptor molecules that end up in the endocytosis of the virion, the fusion of both membranes, and the release of viral RNA in the cytoplasm. This review provides an overview of the targets and progress that has been made in the quest for dengue virus entry inhibitors.

Loading Institute for Scientific Research and Technology Services INDICASAT AIP collaborators
Loading Institute for Scientific Research and Technology Services INDICASAT AIP collaborators