Characterization of Oxidized and Fragmented Superoxide Dismutase Recruited on Liposome Surface

Abstract

The interaction of oxidized and fragmented SOD with liposomes has been reported to induce the original SOD-like enzymatic activity (L.Q. Tuan et al., Langmuir, 24 (2008) 350-354). The effect of several kinds of liposomes on their recruited activity of oxidized and fragmented SOD was first investigated. The addition of zwitterionic liposomes with high membrane fluidity or that with positive charge was found to increase the SOD-like activity of fragmented SOD although the negatively charged liposome has no effect on its activity. The SOD-like activity was found to be related to the adsorbed amount of the peptides on the liposome surface. The analyzed characteristics of the peptide, together with the above findings, imply that the liposome-recruited activity of the fragmented SOD was related with the recognition of the SOD fragment by the liposome caused by the combination of electrostatic and hydrophobic interaction, and hydrogen bonding between the peptide and liposome membrane.

Negatively charged liposome as a potent inhibitor of post-translation during in vitro synthesis of green fluorescent protein

“…It has recently been reported that the activity of fragmented superoxide dismutase (SOD) with no specific conformation and no activity is enhanced under an oxidative stress condition in the presence of liposome prepared by 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) through enhancement of the interaction between the fragmented SOD and the liposome [17][18][19]. It has recently been reported that the liposome itself can affect in vitro gene expression by selecting the green fluorescent protein (GFP) as a reporter protein [20].…”