Structure determination and synthesis of lysine isopeptides influencing on cell proliferation

Abstract

The clavicepamines are lysine-rich basic proteins isolated from saprophytic culture of ergot (Claviceps purpurea), having human pharmacological importance. Based on structure determinations, it was demonstrated that the epsilon-lysine (poly)peptides are the fundamental structural units of clavicepamines. To study the relationship between chemical structure and biological effect, solution and solid-phase synthesis of lysine isopeptides were performed. Poly-epsilon-lysines were synthesized with polycondensation via application of p-nitrophenylester temporarily protecting groups together with simultaneous activation. The biological investigations of poly-epsilon-lysines showed a cell-proliferation retarding effect, so they inhibit growth of some animal tumors, practically without toxic side effects.

Identification of ε-Poly-L-lysine as an Antimicrobial Product from an Epichloë Endophyte and Isolation of Fungal ε-PL Synthetase Gene

“…ε-PL has been known as an antibacterial polyamine secreted mainly by some bacteria in the Streptomycetaceae family [25] and a few members of the Bacillaceae family [26,27]. Production of ε-PL in fungi has also been reported for Clavicipitaceae fungi, including ergot fungi Claviceps purpurea [28] and Epichloë sp. MN-9 [29].…”