Pseudotropine (ψ-tropine, or psi-tropine) is an isomer of tropine. Pseudotropine is formed during NADPH-dependent reduction of the 3-carbonyl group of tropinone to a beta-hydroxyl group. Tropinone reductase-II is an enzyme responsible for this transformation. It is known, that tropinone reductase-II is also a key enzyme in the biosynthetic pathway of tropane alkaloids, which include medicinally important compounds such as hyoscyamine (atropine) and cocaine.

Pseudoyohimbine is an alkaloid isolated from the bark of Corynanthe johimbe and Rauwolfia canescens.

Reserpic acid, a derivative of the antihypertensive drug reserpine, can inhibit norepinephrine uptake although it is much less effective than reserpine itself. Recently was shown, that reserpic acid possessed a strong binding to the pancreatic lipase, a major target for controlling the obesity.

Reserpic acid, a derivative of the antihypertensive drug reserpine, can inhibit norepinephrine uptake although it is much less effective than reserpine itself. Recently was shown, that reserpic acid possessed a strong binding to the pancreatic lipase, a major target for controlling the obesity.

Melezitose is a nonreducing trisaccharide sugar that is produced by many plant sap-eating insects, including aphids such as Cinara pilicornis. Melezitose is beneficial to the insects, as it reduces the stress of osmosis by reducing their own water potential. The melezitose is part of the honeydew which acts as an attractant for ants and also as a food for bees. Melezitose fatty acid monoesters are potential surfactants, that may solubilize hydrophobic drugs for parenteral formulations.

Racemic phenibut (beta-phenyl-gamma-aminobutyric acid or 4-amino-3-phenylbutyric acid) is a neuropsychotropic drug that was discovered and introduced into clinical practice in Russia in the 1960s. In pharmacological tests of locomotor activity, antidepressant and pain effects, S-phenibut was inactive. In contrast, R-phenibut turned out to be two times more potent than racemic phenibut in most of the tests. Racemic phenibut and R-phenibut demonstrated an affinity for GABAB receptors, in contrast, S-phenibut was not able to bind receptors. Pharmacological activity of racemic phenibut relies on R-phenibut and this correlates to the binding affinity of enantiomers of phenibut to the GABAB receptor. Both S- and R-phenibut bind to the α2-δ subunit of voltage-dependent calcium channels and exert gabapentin-like anti-nociceptive effects. In addition S-isomer was found to be a substrate of gamma-aminobutyric acid aminotransferase, however, the R-isomer is a competitive inhibitor.