Biomedical subjects

Reinskje Talhout

Publications and source records attributed to Reinskje Talhout.

5 recordsLinked to original sources

PubMed2006

Sugars as tobacco ingredient: Effects on mainstream smoke composition.

Sugars are natural tobacco components, and are also frequently added to tobacco during the manufacturing process. This review describes the fate of sugars during tobacco smoking, in particular the effect of tobacco sugars on mainstream smoke composition. In natural tobacco, sugars can be present in levels up to 20 wt%. In addition, various sugars are added in tobacco manufacturing in amounts up to 4 wt% per sugar. The added sugars are usually reported to serve as flavour/casing and humectant. However, sugars also promote tobacco smoking, because they generate acids that neutralize the harsh taste and throat impact of tobacco smoke. Moreover, the sweet taste and the agreeable smell of caramelized sugar flavors are appreciated in particular by starting adolescent smokers. Finally, sugars generate acetaldehyde, which has addictive properties and acts synergistically with nicotine in rodents. Apart from these consumption-enhancing pyrolysis products, many toxic (including carcinogenic) smoke compounds are generated from sugars. In particular, sugars increase the level of formaldehyde, acetaldehyde, acetone, acrolein, and 2-furfural in tobacco smoke. It is concluded that sugars in tobacco significantly contribute to the adverse health effects of tobacco smoking.

Acetaldehyde↗

PubMed2006

Contribution of monoamine oxidase (MAO) inhibition to tobacco and alcohol addiction.

Whole-body PET-scan studies in brains of tobacco smokers have shown a decrease in monoamine oxidase (MAO) activity, which reverts to control level when they quit smoking. The observed decrease in MAO activity in smokers is presumably due to their exposure to tobacco constituents that possess MAO-inhibiting properties. The inhibition of MAO activity seems, however, not to be a unique feature of tobacco smoking as subjects with Type II alcoholism have been reported to show a similar decrease in MAO activity that reverses when they cease to use alcohol. The present review summarizes the data on MAO-inhibiting tobacco constituents and explains that the decrease in MAO activity observed in alcoholics is probably due to concomitant tobacco use. It is concluded that the inhibition of MAO by constituents contained in tobacco and tobacco smoke, enhances the addiction induced by tobacco smoking.

Alcoholism↗

PubMed2004

Probing the effect of the amidinium group and the phenyl ring on the thermodynamics of binding of benzamidinium chloride to trypsin.

The effect of the amidinium group and the phenyl ring on the thermodynamics of binding of benzamidinium chloride to the serine proteinase trypsin has been studied using isothermal titration calorimetry. Binding studies with benzylammonium chloride, [small alpha]-methylbenzylammonium chloride and benzamide, compounds structurally related to benzamidinium chloride, showed that hydrogen bonding between the amidinium group and the enzyme is primarily enthalpy-driven. Binding of cyclohexylcarboxamidinium chloride and acetamidinium chloride showed that the hydrophobic binding of the phenyl ring in the S1 pocket is primarily entropy-driven and that a rigid, flat hydrophobic binding site for the inhibitor is favourable. The compounds that have been studied over a range of temperatures exhibit a negative change in heat capacity upon binding and enthalpy-entropy compensation, both characteristic of hydrophobic interactions.

Benzylammonium Compounds↗

PubMed2004

Aggregation behavior of p-n-alkylbenzamidinium chloride surfactants.

The aggregation behavior of a novel class of surfactants, p-n-alkylbenzamidinium chlorides, has been investigated. The thermodynamics of aggregation of p-n-decylbenzamidinium chloride mixed with cationic and anionic cosurfactants has been studied using isothermal titration calorimetry. For mixtures of p-n-decylbenzamidinium chloride with n-alkyltrimethylammonium chlorides, the aggregation process is enthalpically more favorable than for the pure n-alkyltrimethylammonium chlorides, probably caused by diminished headgroup repulsion due to charge delocalization in the amidinium headgroup. A critical aggregation concentration between 3 and 4 mM has been extrapolated for p-n-decylbenzamidinium chloride at 40 degrees C, around two times lower than that of similar surfactants without charge delocalization in the headgroup and well comparable to that of similar surfactants with charge delocalization in the headgroup. In mixtures of p-n-decylbenzamidinium chloride with either sodium n-alkylsulfates or sodium dodecylbenzenesulfonate, evidence is found for the formation of bilayer aggregates by the pseudo-double-tailed catanionic surfactants composed of p-n-decylbenzamidinium and the anionic surfactant. These aggregates are solubilized to mixed micelles by excess free anionic surfactant at the measured critical aggregation concentration.

Journal Article↗

PubMed2003

Understanding binding affinity: a combined isothermal titration calorimetry/molecular dynamics study of the binding of a series of hydrophobically modified benzamidinium chloride inhibitors to trypsin.

The binding of a series of p-alkylbenzamidinium chloride inhibitors to the serine proteinase trypsin over a range of temperatures has been studied using isothermal titration (micro)calorimetry and molecular dynamics simulation techniques. The inhibitors have small structural variations at the para position of the benzamidinium ion. They show small differences in relative binding affinity but large compensating differences in enthalpy and entropy. Binding affinity decreases with increased branching at the first carbon but increases with increasing the length of a linear alkyl substituent, suggesting that steric hindrance and hydrophobic interactions play dominant roles in binding. Structural analysis showed that the backbone of the enzyme was unaffected by the change of the para substituent. In addition, binding does not correlate strongly with octanol/water partition data. To further characterize this system, the change in the heat capacity on binding, the change in solvent-accessible surface area on binding, the effect of inhibitor binding on the hydration of the active site, the pK(a) of His57, and interactions within the catalytic triad have been investigated. Although the changes in inhibitor structure are small, it is demonstrated that simple concepts such as steric hindrance, hydrophobicity, and buried surface area are insufficient to explain the binding data. Other factors, such as access to the binding site and the cost of dehydration of the active site, are of equal or greater importance.

Benzamidines↗