Phytochemical compounds of anise hyssop (Agastache foeniculum) and antibacterial, antioxidant, and acetylcholinesterase inhibitory properties of its essential oil

Agastache foeniculum (Pursh) Kuntze (anise hyssop) is known as a medicinal and flavoring spice plant. The aim ofthis research was gas chromatography-mass spectrometry (GC-MS) analysis of anise hyssop essential oil and analysisof radical scavenging ability, antimicrobial activity, and acetylcholinesterase inhibitory activity. Phytochemicalcomposition of anise hyssop wastes and the aqueous extract obtained after steam distillation was investigated.Eight compounds were identified in essential oils by GC-MS analysis, as the major ones were phenylpropenoids[estragol—93.45% of total ion current (TIC), eugenol—0.15% of TIC, and methyl isoeugenol—2.48% of TIC]. Inthe anise hyssop wastes extract, four pentacyclic triterpenes were identified (betulin—36.1 mg/g, betulinic acid—2.4mg/g, oleanolic acid—160.0 mg/g, and ursolic acid—6.7 mg/g extract). Rosmarinic acid (50.6 mg/g extract) andflavonoids—myricetin (0.5 mg/g), luteolin (0.9 mg/g), and apigenin (0.6 mg/g) were detected by high-performanceliquid chromatography with diode-array detection analysis of aqueous extract. The anise hyssop essential oil showedstrong radical scavenging ability IC50—6.54 μl/ml. The results obtained from antimicrobial screening revealed thatessential oil possessed inhibitory activity against Staphylococcus aureus ATCC 25923, Curtobacterium flaccumfaciensPM_YT, Listeria monocytogenes, Bacillus subtilis ATCC 6633, Salmonella sp., Escherichia coli ATCC 8739, Proteusvulgaris, Pseudomonas aeruginosa ATCC 9027, Klebsiella pneumoniae, and Candida albicans, while Enterococcusfaecalis remained unaffected.

Gen de la calcitonina: síntesis química y expresión en Escherichia coli / Human calcitonine gene: chemical synthesis and expression in Escherichia coli

La calcitonina es una hormona polipéptida de 32 aminoácidos que interviene en la regulación del metabolismo del fósforo y el calcio en los vertebrados. En este trabajo presentamos los resultados de la síntesis química y la expresión directa de los genes humanos de calcitonina en E. coli. Para evitar la acción recombinante de la calcitonina contra proteasas bacteriales, se construyó una serie de genes oligómeros de calcitonina que codifican proteínas multidominio con un número variable de monómeros. Se expresaron bajo el control de un promotor fuerte sintético y en un sitio de unión al ribosoma, y se encontró que en el gen de calcitonina tetrámera daba un producto estable del 13 % de rendimiento del total de la proteína bacteriana. La calcitonina recombinante multidominio puede pasar a forma monómera mediante tratamiento con BrCN