Abstract

The fluid mosaic model of Singer and Nicolson in 1972 shows how proteins are embedded in membranes. To elucidate the interactions between proteins and the surrounding lipids, stearic acid (SA) and bovine serum albumin (BSA) were used as lipid-protein components to mimic the normal membrane bilayer environment using the Langmuir-Blodgett technique. Surface pressure (π)-molecular area (A) isotherms were recorded for the SA monolayer in the presence of BSA on water. The mixed monolayer was successfully transferred onto an oxidized silicon wafer and imaged by tapping mode atomic force microscopy (AFM). Miscibility, compressibility and thermodynamic stability of the mixed system were examined. A large negative deviation of Aex, together with the minimum value of ΔGex, was observed when the mole fraction of BSA (XBSA) was 0.8, indicating this to be the most stable mixture. In a compressibility analysis, XBSA was observed at below 50 mN m-1, denoting a liquid-expanded phase and showing the occurrence of a strong interaction of SA with BSA molecules in this phase. AFM observations supported the quantitative data indicating that BSA was strongly attracted onto the membrane surface as predicted.

Highlights

  • Immunoliposomes have been extensively developed for its potential as drug delivery carriers by attaching antibodies to the liposomal surface

  • There are several proposed drugloaded immunoliposome formulations that are used in drug delivery applications [5,6,7,8], but there is still scant knowledge on how liposomes interact with the antibodies they incorporate [9,10]

  • When bovine serum albumin (BSA) was incorporated into the stearic acid (SA) monolayer, the shape of the π-A isotherm gradually changed with increasing concentrations of BSA

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Summary

Introduction

Immunoliposomes have been extensively developed for its potential as drug delivery carriers by attaching antibodies to the liposomal surface. Many in vitro studies using immunoliposomes in drug delivery to target cancer cells have greatly showed significant reduction in toxicities and improved therapeutic efficacy [1,2,3,4]. This promising approach can overcome challenges of targeting only the cancer and tumour cells that are often very similar in characteristics to the surrounding healthy tissue. There are several proposed drugloaded immunoliposome formulations that are used in drug delivery applications [5,6,7,8], but there is still scant knowledge on how liposomes interact with the antibodies they incorporate [9,10].

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