Predictive quantitative structure-activity relationships (QSAR) analysis of beta 3-adrenergic ligands.

A novel quantitative structure-activity relationships strategy was used to analyze seventeen beta-adrenergic ligands for which we had previously evaluated pharmacological properties in Chinese hamster ovary cells transfected with the human beta 1-, beta 2- or beta 3-adrenergic gene (Blin et al., 1993, Mol. Pharmacol.

Use of TSAR as a new tool to analyze the molecular dynamics trajectories of proteins.

There is a lack of tools to analyze simulations of protein molecular dynamics quantitatively. Our aim is to use calmodulin, a prototypical calcium-binding protein, to describe a strategy and some tools for extracting relevant information from dynamics calculations. Our main conclusions are as follows: Autocorrelation vectors may be used to represent a 3D conformation in an n-dimensional space, where n is variable (n < or = 20-30).

Quantitative autoradiographic mapping of 5-HT3 receptors in the rat CNS using [125I]iodo-zacopride and [3H]zacopride as radioligands.

Substitution of the chlorine atom by a radio-iodine in position 5 in the zacopride molecule yielded [125I]iodo-zacopride that bound with high affinity (Kd = 4.3 nM) to 5-HT3 receptors in the rat central nervous system. Assays with membranes from the posterior (mainly entorhinal) cortex confirmed that the pharmacological properties and regional distribution of [125I]iodo-zacopride-specific binding sites were identical with those of 5-HT3 sites labelled by the reference radioligand [3H]zacopride.

[(125I)iodo-zacopride: new ligand for the study by autoradiography of central 5-HT3 receptors].

This paper describes the synthesis and the pharmacological characteristics of the first radioiodinated ligand of central 5-HT3 receptors: [125I]iodo-zacopride. Specific sites having a high affinity (Kd = 4.3 nM) for [125I]iodo-zacopride have been found in membranes from the rat entorhinal cortex.