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Antibacterial activity of metal complexes of benzil and benzoin thiosemicarbazones.

The metal (II) complexes of benzyl and benzoin thiosemicarbazones have been synthesized and characterized. They were studied for their antibacterial, antifungal and amoebicidal activity in vitro and for their toxicity in vivo. The ligands and their metal complexes exhibited low antibacterial and amoebicidal activity. The metal chelates of benzoin thiosemicarbazone seem to be the most active compounds.

Animals↗
PubMed1986

Multiple binding affinities of N-methylscopolamine to brain muscarinic acetylcholine receptors: differentiation from M1 and M2 receptor subtypes.

The properties of the specific binding of the muscarinic receptor ligands [3H]quinuclidinyl benzilate and N-[3H]methylscopolamine in rat brain were compared. The specific binding of both ligands was affected equally by heat, phospholipase A2 and trypsin. N-[3H]methylscopolamine labeled only a fraction of the total muscarinic receptors recognized by [3H]quinuclidinyl benzilate in different brain areas and in the heart. Evidence is presented that N-[3H]methylscopolamine, in fact, binds to a subpopulation of [3H]quinuclidinyl benzilate binding sites. The distribution of the high-affinity binding sites of N-[3H]methylscopolamine did not show a different tissue dependence as compared to the total receptor population, and did not parallel the distribution of the pirenzepine-sensitive M1 receptor subtype. Similarly, the affinity of both [3H]quinuclidinyl benzilate and N-[3H]methylscopolamine varied from one tissue to another by a maximum of 2-fold. Although (-)-quinuclidinyl benzilate competed for the specific binding of [3H]quinuclidinyl benzilate in different tissues according to the law of mass-action, N-methylscopolamine showed an anomalous interaction with two binding sites. The low-affinity binding sites of N-methylscopolamine showed saturability of [3H]quinuclidinyl benzilate binding and stereoselectivity. When the binding characteristics of these N-methylscopolamine-inaccessible binding sites of [3H]quinuclidinyl benzilate in the brain were investigated further, it was found that N-methylscopolamine bound exclusively with a single low affinity, whereas pirenzepine still interacted with two receptor populations incorporated in these sites. It is concluded from several lines of evidence that the heterogeneity of binding of N-methylscopolamine to muscarinic receptors does not represent an interaction with the muscarinic M1 and M2 receptor subtypes defined by pirenzepine. Thus, the unique binding profile of pirenzepine to muscarinic receptors cannot be explained merely on the basis of its hydrophilic nature.

Animals↗
PubMed1979

An 125I-labeled binding probe for the muscarinic cholinergic receptor.

We describe the synthesis and characterization of [125I]3-quinuclidinyl-(3-iodo-4-hydroxy-benzilate), a binding probe for the muscarinic cholinergic receptor of high specific radioactivity. The binding isotherm of this 125I-labeled compound to a rat synaptic plasma membrane-enriched fraction consists of two components: a 'specific' component which is saturable and closely fits hyperbolic binding to a single class of sites as evaluated by Scatchard analysis (Kd = 1.5 to 3 nM), and a linear component which may be measured directly by preincubating membranes in 0.1 microM 3-quinuclidinyl-benzilate, the most potent muscarinic antagonist known. The specific binding of [3-3H]3-quinuclidinyl-benzilate and [125I]3-quinuclidinyl-(3-iodo-4-hydroxy-benzilate) to rat brain subcellular fractions is parallel in myelin, synaptic plasma membrane and mitochondrial fractions with a 3--4-fold enrichment observed in synaptic plasma membrane over crude mitochondrial fractions. The concentrations of muscarinic antagonists required to block [125I]3-quinuclidinyl-(3-iodo-4-hydroxy-benzilate) binding parallel that reported for tritiated binding probes and are consistent with physiological measurements of their dissociation constants. Because of the high specific radioactivity of [125I]3-quinuclidinyl-(3-iodo-4-hydroxy-benzilate), this iodinated binding probe should prove useful in assaying low levels of muscarinic receptor in tissue culture and other biological sources.

Animals↗