Study on the interaction of Prodigiosin with bovine serum albumin by spectroscopic methods

Shu-Chao Liu,Jing Tang,Xi-Hai Zhang,Qi-Yin Yang,Yuan-Yuan Gao,Fei Ma

doi:10.1155/2012/797132

Abstract

The interaction between bovine serum albumin (BSA) and Prodigiosin (PG) was investigated by UV-vis absorption, fluorescence, synchronous fluorescence, FT-IR and circular dichroism (CD) techniques. The data of UV-vis absorption and fluorescence spectra displayed that there existed interaction between PG and aromatic amino acid residues of BSA. The synchronous fluorescence and CD spectrum experiment both showed that the secondary structure of BSA changed with addition of PG. All these results revealed that the conformation and microenvironment of BSA were changed.

Highlights

Prodigiosin (PG) (Scheme 1) is a red, linear tripyrrole and a member of the prodiginines, produced by some Serratia sp., Actinomycetes and a few other Bacteria [12]
The absorption of bovine serum albumin (BSA) at 278 nm increased obviously with the addition of PG, the reason stem from the interaction between PG and aromatic amino acid residues in BSA molecular external, the results indicated that the Oxygen groups in PG interacted with the oxygen groups or nitrogen groups in the amino acid residues of BSA peptide chain, which led to the microenvironment of BSA changed in the interaction
This paper presented spectroscopic studying on the interaction of PG with BSA using UV/vis spectrum, fluorescence emission spectrum, synchronous fluorescence spectrum, FT-IR spectrum and circular dichroism spectrum

Summary

Introduction

Prodigiosin (PG) (Scheme 1) is a red, linear tripyrrole and a member of the prodiginines, produced by some Serratia sp., Actinomycetes and a few other Bacteria [12]. Prodigiosin is classical secondary metabolites only appearing in later stages of bacterial growth [27]. Prodigiosin itself has considerable immunosuppressive activity, antibacterial, antimycotic and antimalarial activity, etc. The US National Cancer Institute (NCI) confirmed that PG had a stronger resistibility to 57 various human cancer cells such as in vitro liver cancer transfer and primary cancer cells, PG had not obvious toxicity to nonmalignant celllines [8]. Serum albumin is the major protein constituent of blood plasma which facilitates the disposition and transportation of various exogenous and endogenous ligands to the specific targets [16].

Methods

Results

Conclusion