Chemical Constituents from Sambucus adnata and Their Protein–Tyrosine Phosphatase 1B Inhibitory Activities

• Published in: Chemical & pharmaceutical bulletin Vol. 59; no. 11; pp. 1396 - 1399
• Main Authors: Sasaki, Tatsunori, Li, Wei, Morimura, Haruna, Li, Songpei, Li, Qin, Asada, Yoshihisa, Koike, Kazuo
• Format: Journal Article
• Language: English
• Published: TOKYO The Pharmaceutical Society of Japan 01.11.2011; Pharmaceutical Soc Japan
• Subjects: Caprifoliaceae; Chemistry; Chemistry, Medicinal; Chemistry, Multidisciplinary; Enzyme Activation - drug effects; Enzyme Inhibitors - chemistry; Enzyme Inhibitors - isolation & purification; Enzyme Inhibitors - pharmacology; Kinetics; Life Sciences & Biomedicine; Magnetic Resonance Spectroscopy; Molecular Conformation; Pharmacology & Pharmacy; Physical Sciences; Protein Tyrosine Phosphatase, Non-Receptor Type 1 - antagonists & inhibitors; Protein Tyrosine Phosphatase, Non-Receptor Type 1 - metabolism; protein–tyrosine phosphatase 1B; Sambucus - chemistry; Sambucus adnata; Science & Technology; triterpene; Triterpenes - chemistry; Triterpenes - isolation & purification; Triterpenes - pharmacology; Sambucus adnata; triterpene; Caprifoliaceae; protein-tyrosine phosphatase 1B; OBESITY; PTP1B; INSULIN-RESISTANCE; NUCLEAR-MAGNETIC-RESONANCE; LIGNANS; TRITERPENES; OLEANOLIC ACID
• ISSN: 0009-2363; 1347-5223; 1347-5223
• DOI: 10.1248/cpb.59.1396

The MeOH extract from the whole plants of Sambucus adnata has shown significant protein–tyrosine phosphatase 1B (PTP1B) inhibitory activity. Chemical study on the extract resulted in the isolation of thirteen compounds, including a novel triterpene (1). The structure of 1 was determined to be 1α,3β-dihydroxy-urs-12-en-11-one-3-yl palmitate on the basis of extensive spectroscopic analyses. Among the isolated compounds, ursolic acid, oleanolic acid and (±)-boehmenan showed the most potent PTP1B inhibitory activity in vitro with the IC50 values of 4.1, 14.4 and 43.5 μm, respectively. The kinetic analysis indicated that (±)-boehmenan inhibits PTP1B activity in a competitive manner.