Fibrinogen-Binding Peptide (designed by anticomplementarity hypothesis) is a presumptive peptide mimic of the vitronectin binding site on the fibrinogen receptor. Fibrinogen, a soluble plasma protein, is a cofactor in platelet activation. It is converted to fibrin in a reaction catalyzed by thrombin.

Dieugenol is a neolignan that has been found in N. leucantha and has antioxidative and antiprotozoal activities. It inhibits the formation of thiobarbituric acid reactive substances (TBARS) and scavenges superoxide anions, but not hydroxyl radicals, in cell-free assays. It has anti-trypanosomal activity against T. cruzi amastigotes and trypomastigotes (IC50s=15.1 and 11.5 μM, respectively) but is cytotoxic to NCTC L-929 fibroblasts with a 50% cytotoxic concentration (CC50) value of 58.2 μM.2 Dieugenol (15 μM) disrupts the integrity of the T. cruzi trypomastigote plasma membrane but does not induce the production of reactive oxygen species (ROS) in trypomastigotes or LPS-stimulated and unstimulated isolated mouse peritoneal macrophages.

(R)-Apremilast is the enantiomer of Apremilast and one of the isoindoline derivatives.