On-line Method for Montelukast Determination in Bile Salt Medium with Multivariate Optimization and Fluorescent Detection

Journal of Analytical Chemistry - The present development involved a flow injection strategy using a mini-column of multiwalled carbon nanotubes and fluorescent detection (λex of 283 nm,...     

Thermodynamic study of transthyretin association (wild‐type and senile forms) with heparan sulfate proteoglycan: pH effect and implication of the reactive histidine residue

The tetramer destabilization of transthyretin into monomers and its fibrillation are phenomena leading to amyloid deposition. Heparan sulfate proteoglycan (HSPG) has been found in all amyloid deposits. A chromatographic approach was developed to compare binding parameters between wild‐type transthyretin (wtTTR) and an amyloidogenic transthyretin (sTTR). Results showed a greater affinity of sTTR for HSPG at pH 7.4 compared with wtTTR owing to the monomeric form of sTTR. Analysis of the thermodynamic parameters showed that van der Waals interactions were involved at the complex interface for both transthyretin forms. For sTTR, results from the plot representing the number of protons exchanged vs pH showed that the binding mechanism was pH‐dependent with a critical value at a pH 6.5. This observation was due to the protonation of a histidine residue as an imidazolium cation, which was not accessible when TTR was in its tetrameric structure. At pH >6.5, dehydration at the binding interface and several contacts between nonpolar groups of sTTR and HSPG were also coupled to binding for an optimal hydrogen‐bond network. At pH <6.5, the protonation of the His residue from sTTR monomer when pH decreased broke the hydrogen‐bond network, leading to its destabilization and thus producing slight conformational changes in the sTTR monomer structure. Copyright © 2014 John Wiley & Sons, Ltd.     

Knowing and Teaching Middle School Mathematics: A Professional Development Course for In‐Service Teachers

This article describes a professional development course intended to improve the content understanding of middle school mathematics teachers. The design of the course included three professional learning strategies: problem solving, examination of student thinking, and discussion of research. The concepts studied in the course included multi‐digit subtraction, multi‐digit multiplication, operations with fractions, and concepts of area and perimeter. Results from pre‐ and post‐tests administered to the nineteen participants indicate a significant increase in the mean score for each concept and document growth in the teachers' content understanding. In particular, their solutions moved from primarily procedural to more conceptual. Responses to an open‐ended survey indicate other important aspects of the professional development. Examples of teachers' work and comments are included.     

Dynamics of kinks in biological membranes

kinks created in a biological membrane by the interaction with a movable bead. We arrive at the evolution equations for both the bead and the membrane, whence we conclude that the force exerted on the bead by a fixed membrane points in the direction along which the curvature of the membrane is more concentrated. This is the first step towards understanding the basic mechanism behind the dynamics of protein aggregation which takes place on biological membranes. Received November 6, 2001 / Published online February 4, 2002     

Calculation of cyclodextrin-mediated enantiomer ratio shifting of racem norgestrel in aqueous solutions

Enantioselective solubility of rac-norgestrel was found in the presence of γ-cyclodextrin or hydroxypropyl-γ-cyclodextrin. In both cases the efficacious enantiomer was dissolved in greater extent. Calculating the molar absorptivity and molar ellipticity spectra of the γ- and hydroxypropyl-γ-cyclodextrin aqueous complexes, a simple and rapid direct circular dichroism (CD) spectrometric method was obtained for the determination of the enantiomer ratio in aqueous solutions.