In vitro and in vivo anti-tumor characterizations of β-elemene-loaded nanoemulsion

Abstract

active targeting drug delivery. Herein LyP-1 peptide was used as a model peptide to verify this phenomenon. LyP-1, a short peptide cyclized with a disulfide bond, can specifically bind to tumor cells through the interaction with cell-surface protein p32/gC1qR. It has been frequently used as a ligand for designing tumor targeted drug delivery systems. However, the instability of disulfide bond limits its potential efficiency. In the present research, we mutated the C-terminal Cys to Ala and cyclized the peptide with an amide bond using native chemical ligation technique. The new cyclic LyP-1 peptide, termed c(LyP-1), has been compared with LyP-1 for their biological functions in cellular levels. Because of the substitution of cyclization from disulfide bond to amide bond, c(LyP-1) modified liposomes showed 3 times enhancement of in vitro targeting capacity to tumor cells when compared with that of LyP-1.