Autofluorescence of MDA-modified proteins as an in vitro and in vivo probe in oxidative stress analysis

Min Qiang,Yajie Xu,Ying Liu,Rongqiao He,Chanshuai Han,Yingge He,Yang Lu

doi:10.1007/s13238-014-0052-1

Abstract

Autofluorescence of MDA-modified proteins as an in vitro and in vivo probe in oxidative stress analysis

Highlights

Malondialdehyde (MDA) is regarded as a biomarker for oxidative stress (Del Rio et al, 2005; Stancliffe et al, 2011), and is generated in the oxidative degradation process of polyunsaturated lipids (Stancliffe et al, 2011)
In order to investigate the effect of MDA-modification on protein aggregation, we generated modified BSA (mBSA) and analyzed its behaviour by SDS-PAGE
After incubation of bovine serum albumin (BSA) with different concentrations of MDA, and subsequent removal of un-incorporated MDA by ultrafiltration, mBSA was analyzed by 12% SDS-PAGE and Coomassie brilliant blue staining of the gel (Fig. 1)

Summary

Introduction

Malondialdehyde (MDA) is regarded as a biomarker for oxidative stress (Del Rio et al, 2005; Stancliffe et al, 2011), and is generated in the oxidative degradation process of polyunsaturated lipids (Stancliffe et al, 2011). After incubation of BSA with different concentrations of MDA, and subsequent removal of un-incorporated MDA by ultrafiltration, mBSA was analyzed by 12% SDS-PAGE and Coomassie brilliant blue staining of the gel (Fig. 1). The modified proteins appeared to form a polymeric structure (Fig. 1C and 1D), while no polymers were visible in the unmodified BSA samples (Fig. 1E).

Results

Conclusion