Screening and analysis of anionic peptides from Foeniculum vulgare Mill by mass spectroscopy

Abstract EN

Fennel (Foeniculum vulgare Mill.) member from the family Umbelliferae (Apiaceae) and has been used in Saudi Arabia as an medicine as of the from the tradition.

Our previous work with seed extracts of this plant generated DEAE-ion exchange purified proteins that exhibited antibacterial properties.

The current study moves this work forward by using 2-D gel separation and MALDI TOF/TOF to identify proteins in this active extract.

Fourteen protein spots were excised, digested, and identified.

Several putative functions were identified, including: a copper-trans locating ATPase PAA1 chloroplastic-like isoform X1; a cytosolic enolase; a putative pentatricopeptide repeat-containing protein; an NADP-requiring isocitrate dehydrogenase; two proteins annotated as being encoded downstream from Son-like proteins; three probable nuclear proteins 5–1; and four predicted/ unidentified proteins.

Future efforts will further characterize their relevant antimicrobial properties with the aim of cloning and high throughput synthesis of the antimicrobial element(s).