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  • Chemical probes of a trisubstituted pyrrole to identify its protein target(s) in Plasmodium sporozoites.

Chemical probes of a trisubstituted pyrrole to identify its protein target(s) in Plasmodium sporozoites.

Bioorganic & medicinal chemistry letters (2013-02-12)
Tyrell Towle, Isabell Chang, Isabel Chang, Robert J Kerns, Purnima Bhanot
ZUSAMMENFASSUNG

Malaria is a disease that has a major impact in many developing nations, especially on the African continent. There is a need to develop new therapeutics and prophylactic treatments against it. A trisubstituted pyrrole was recently found to inhibit infection of mammalian hepatocytes by Plasmodium sporozoites, but the target of this agent is not known. In this study trisubstituted pyrrole derivatives with different substituents on a piperidinyl nitrogen were prepared. We determined if modifications of the piperidinyl nitrogen would accommodate a drug-biotin linking strategy for affinity purification of the trisubstituted pyrrole's target protein(s).

MATERIALIEN
Produktnummer
Marke
Produktbeschreibung

Sigma-Aldrich
Piperidin, ReagentPlus®, 99%
Sigma-Aldrich
Piperidin, ≥99.5%, purified by redistillation
Sigma-Aldrich
Piperidin, biotech. grade, ≥99.5%
Sigma-Aldrich
Piperidin -Lösung, suitable for peptide synthesis, 20% in DMF