Piericidin A

• CAT Number: R001881
• CAS Number: 2738-64-9
• Molecular Formula: C25H37NO4
• Molecular Weight: 415.60
• Purity: ≥95%
• Synonyms: 2-[(2E,5E,7E,9R,10R,11E)-10-Hydroxy-3,7,9,11-tetramethyl-2,5,7,11-tridecatetraen-1-yl]-5,6-dimethoxy-3-methyl-4-pyridinol
• Target: Antibody-drug Conjugate/ADC Related
• Solubility: Soluble in DMSO
• Storage: -20°C
• IUPAC Name: 2-[(2E,5E,7E,9R,10R,11E)-10-hydroxy-3,7,9,11-tetramethyltrideca-2,5,7,11-tetraenyl]-5,6-dimethoxy-3-methyl-1H-pyridin-4-one
• InChI: InChI=1S/C25H37NO4/c1-9-18(4)22(27)19(5)15-17(3)12-10-11-16(2)13-14-21-20(6)23(28)24(29-7)25(26-21)30-8/h9-10,12-13,15,19,22,27H,11,14H2,1-8H3,(H,26,28)/b12-10+,16-13+,17-15+,18-9+/t19-,22+/m1/s1
• InChIKey: BBLGCDSLCDDALX-LKGBESRRSA-N
• SMILES: C/C=C(\C)/[C@@H]([C@H](C)/C=C(\C)/C=C/C/C(=C/CC1=C(C(=O)C(=C(N1)OC)OC)C)/C)O

Piericidin A（Cat No.:R001881）is a naturally occurring antibiotic derived from Streptomyces species, known for its potent inhibitory effects on mitochondrial electron transport. Structurally similar to coenzyme Q, Piericidin A specifically targets Complex I in the respiratory chain, disrupting cellular respiration in bacteria and some eukaryotic cells. This makes it valuable in biochemical research focused on energy metabolism, oxidative phosphorylation, and cellular bioenergetics. Beyond its research applications, Piericidin A is also being studied for potential antifungal, insecticidal, and anticancer properties, as its mechanism holds promise for developing targeted therapeutic agents.

Reference

Evidence for a quinone binding site close to the interface between NUOD and NUOB subunits of Complex I. Prieur I. et al. Biochim. Biophys. Acta 2001, 1504, 173.




H+/2e- stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles. Galkin A.S. et al. FEBS Lett. 1999, 451, 157.


The 49-kDa subunit of NADH-ubiquinone oxidoreductase (Complex I) is involved in the binding of piericidin and rotenone, two quinone-related inhibitors. Darrouzet E. et al. FEBS Lett. 1998, 10, 34.

Two binding sites of inhibitors in NADH: ubiquinone oxidoreductase (complex I). Relationship of one site with the ubiquinone-binding site of bacterial glucose:ubiquinone oxidoreductase. Friedrich T. et al. Eur J Biochem. 1994, 219, 691.