PEGylation of bovine serum albumin using click chemistry for the application as drug carriers.

Abstract

Monomethyl poly(ethylene glycol) (mPEG)-modified bovine serum albumin (BSA) conjugates (BSA-mPEG) were obtained by the mild Cu(I)-mediated cycloaddition reaction of azided BSA (BSA-N(3) ) and alkyne-terminated mPEG. The structure and characteristics of BSA-mPEG conjugates were thoroughly investigated. There were about two PEG chains conjugated onto each BSA molecule as determined by matrix-assisted laser desorption/ionization time of flight (MALDI-TOF) analysis. The intrinsic nonspecific binding ability of BSA was used for adsorption and sustained release of both rifampicn and 5-fluorouracil (5-FU). The helical structures of BSA were preserved to a large extent after modification and drug adsorption on BSA was confirmed via circular dichroism spectroscopy. Drugs adsorbed onto the conjugated formulation to a lesser extent than on BSA due to mPEG modification. The in vitro release of both rifampicin and 5-FU, however, indicated that BSA-mPEG can function as a drug carrier. Overall, the click reaction provided a convenient tool for the pegylation of BSA. The biological activity of the BSA-mPEG conjugates, including the drug transportation capacity and biocompatibility, were largely retained.

DOI: 10.1002/btpr.1526

7 Figures and Tables

Cite this paper

@article{Li2012PEGylationOB, title={PEGylation of bovine serum albumin using click chemistry for the application as drug carriers.}, author={Xiao-yuan Li and Tai-Hang Li and Jin-Shan Guo and Ying Wei and Xia-bin Jing and Xue-si Chen and Yu-Bin Huang}, journal={Biotechnology progress}, year={2012}, volume={28 3}, pages={856-61} }