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Biomedical subjects

A M Pimenta

Publications and source records attributed to A M Pimenta.

5 recordsLinked to original sources
PubMed2005

Application of sequential injection analysis to pharmaceutical analysis.

Sequential injection analysis is a well established tool for automation of pharmaceutical analysis. A short historical background of this technique is given as well as a brief discussion on the basic principles and potentials. The current applications of SIA in the pharmaceutical analysis are also described and discussed. The manifolds developed offer good analytical characteristics and are suitable for analysis of drug formulations, process analysis, drug-dissolution, drug-release testing and functional assays for screening potential drugs. The results obtained are in good agreement with those furnished by the application of the reference methods presented in the pharmacopoeias.

Biological Availability↗
PubMed2001

Moving pieces in a proteomic puzzle: mass fingerprinting of toxic fractions from the venom of Tityus serrulatus (Scorpiones, Buthidae).

Scorpion venoms are very complex mixtures of molecules, most of which are peptides that display different kinds of biological activity. These venoms have been studied in the light of their pharmacological targets and their constituents are able to bind specifically to a variety of ionic channels located in prey tissues, resulting in neurotoxic effects. Toxins that modulate Na(+), K(+), Ca(++) and Cl(-) currents have been described in scorpion venoms. Mass spectrometry was employed to analyze toxic fractions from the venom of the Brazilian scorpion Tityus serrulatus in order to shed light on the molecular composition of this venom and to facilitate the search for novel pharmacologically active compounds. T. serrulatus venom was first subjected to gel filtration to separate its constituents according to their molecular size. The resultant fractions II and III, which account for 90 and 10% respectively of the whole venom toxic effect, were further analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS), on-line liquid chromatography/electrospray mass spectrometry (LC/ESMS) and off-line LC/MALDI-TOFMS in order to establish their mass fingerprints. The molecular masses in fraction II were predominantly between 6500 and 7500 Da. This corresponds to long-chain toxins that mainly act on voltage-gated Na(+) channels. Fraction III is more complex and predominantly contained molecules with masses between 2500 and 5000 Da. This corresponds to the short-chain toxin family, most of which act on K(+) channels, and other unknown peptides. Finally, we were able to measure the molecular masses of 380 different compounds present in the two fractions investigated. To our knowledge, this is the largest number of components ever detected in the venom of a single animal species. Some of the toxins described previously from T. serrulatus venom could be detected by virtue of their molecular masses. The interpretation of this large set of data has provided us with useful proteomic information on the venom, and the implications of these findings are discussed.

Amino Acid Sequence↗
PubMed2001

Clavulanate-selective electrodes--application to pharmaceutical formulations.

The construction and assessment of a clavulanate anion-selective electrode and its application to the analysis of pharmaceutical formulations by direct potentiometry are described. The electrode, prepared without inner reference solution, was fabricated by use of a PVC membrane, with bis(triphenyl-phosphoranylidene)ammonium clavulanate as ion-exchanger dissolved in 2-nitrophenyl octyl ether as intermediate solvent and p-t-octylphenol as additive. The response of the electrode was linearly dependent on concentration within the range 2.4 x 10(-3)-1 x 10(-1) mol dm(-3) (ionic strength adjusted to 0.1 mol dm(-3)); the slope of the calibration plot was -59.4+/-0.9 mV decade(-1) and the reproducibility +/-0.6 mV day(-1). The response time was less than 20 s. Relative errors were <3.5% when results from analysis by direct potentiometry were compared with those from the reference method.

Anti-Bacterial Agents↗
PubMed2001

Purification, amino-acid sequence and partial characterization of two toxins with anti-insect activity from the venom of the South American scorpion Tityus bahiensis (Buthidae).

We report here the isolation by a two-step chromatographic procedure of two new toxins from the South American scorpion Tityus bahiensis. Their amino-acid sequences and some of their biological features were established. The two toxins have different biological properties. Toxin TbIT-I had almost no activity or pharmacological effects in vertebrate tissues whereas it was lethal to house flies (LD50 80.0 ng/house fly). In contrast, Tb2-II was active against both mammals (intracerebroventricular injection of 100 ng/mouse was lethal) and insects (LD50 40.0 ng/house fly). The amino-acid sequences of these toxins were established and found to be similar (60-95%) to previously described beta-toxins from the Tityus genus. Based on the available comparative information, this study attempts identify possible structure-function relationships that may be responsible for the differences in bioactivity displayed by these toxins.

Amino Acid Sequence↗