Positioning, labelling and control of medical information: artesunate strategy and Arsumax development story.

Sanofi decided, some years ago, to help developing a molecule of a new type called artesunate, a semisynthetic derivative from Qinghaosu, or artemisinine, a sesquiterpenic lactone extracted from the leaves of a world wide spread plant: Artemisia annua. After having signed a secrecy agreement with a local pharmaceutical company in China manufacturing artesunate, Sanofi started, in 1993, the assessment of all the data transmitted as well as the plant involved in the artesunate tablet manufacturing. As conclusions of the whole audit performed on this project were judged satisfactory, Sanofi signed a cooperation agreement with this Chinese pharmaceutical firm in order to be allowed to start further development work required to guarantee quality and safety of artesunate 50 mg tablets called Arsumax, and to complete a registration dossier acceptable for Health Authorities in French-speaking Africa. Pharmaceutical, pharmacotoxicological and clinical documentation were widely completed, and entirely reformated according to European guidelines. The registration dossier was submitted in all French speaking African countries. The approval has been obtained in 13 countries. Due to its fast efficacy, its absence of undesirable effects, its presentation in tablets, its quite simple dosage (one box for a treatment), Arsumax positioned itself as an accurate second line antimalaric treatment.

Transport and hydrolysis of peptides in Saccharomyces cerevisiae.

The transport and hydrolysis of several radioactive di- and tripeptides in Saccharomyces cerevisiae was studied. A peptide-transport-deficient mutant isolated on the basis of its resistance to nikkomycin Z lost most of its capacity to take up di- and tripeptides. The transport kinetics of [14C]methionylglycine, [14C]methionylsarcosine and [3H]nikkomycin Z indicated that peptide transport is not dependent on intracellular hydrolysis. Intact cells had some peptidase activity towards methionylsarcosine but not towards nikkomycin Z. The relationship between this activity and peptide transport is discussed.