HYDROPHOBIC CHAINS OF THE PEPLIPOID REGULATE THE BEHAVIOR OF THE LIPOSOME COMPLEXES IN VIVO

Baoquan Liu, Shengdi Fan, Liying Zhang and Chunshan Quan

Key Lab of Biotechnology and Biosource Utilization, Ministry of Education, Dalian Minzu University, Dalian, 116600, China

Abstract

Novel peplipoid designed and synthesized by our group belongs to the artificial lipid which is derived from peptides or amino acid. Its basic structure is made up of three domains: hydrophobic chains, backbone and hydrophilic head, and these domains are mainly linked with amide bonds. When the peplipoid self-assembled into liposome, hydrogen bonds formed between the amide bonds of the peplipoid would enhance the stability of the liposome.

A series of peplipoid contained asymmetric double hydrophobic chains are designed and synthesized with lysine as backbone, and used to verify the function of different hydrophobic chains in vivo. The green fluorescent protein (GFP) gene is used to report the behavior of the complexes of liposome and DNA. The results show that all the complexes can delivery DNA into cell nucleus and express the reporter gene. When the GFP is changed to luciferase gene, different transfection efficiencies are obtained with the complexes contained different peplipoid. the best transfection efficiency is obtained when the peplipoid with C_18:2 hydrophobic chain is used to assemble the complexes of liposome and DNA. This result shows asymmetric hydrophobic chain changes the behavior of the complexes of liposome and DNA in vivo.

Keywords: Peplipoid, hydrophobic chain, liposome.

*Supported by Natural Science Foundation of China (21172028, 21272031, 21372037).