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Formulation and Engineering of Biomaterials
PEGylation of bovine serum albumin using click chemistry for the application as drug carriers
Article first published online: 28 FEB 2012
DOI: 10.1002/btpr.1526
Copyright © 2012 American Institute of Chemical Engineers (AIChE)
Additional Information
How to Cite
Li, X.-Y., Li, T.-H., Guo, J.-S., Wei, Y., Jing, X.-B., Chen, X.-S. and Huang, Y.-B. (2012), PEGylation of bovine serum albumin using click chemistry for the application as drug carriers. Biotechnol Progress, 28: 856–861. doi: 10.1002/btpr.1526
Publication History
- Issue published online: 9 JUN 2012
- Article first published online: 28 FEB 2012
- Accepted manuscript online: 24 JAN 2012 05:00PM EST
- Manuscript Revised: 17 JAN 2012
- Manuscript Received: 29 SEP 2011
Funded by
- National Natural Science Foundation of China. Grant Numbers: 50733003, 51021003, 20874097
- Ministry of Science and Technology of China. Grant Number: 973 Project, No. 2009CB930102
- “100 Talents Program” of the Chinese Academy of Sciences. Grant Number: KGCX2-YW-802
- Jilin Provincial Science and Technology Department. Grant Numbers: 20082104, 20100588
Keywords:
- bovine serum albumin;
- mPEG;
- click chemistry;
- rifampicin;
- 5-fluorouracil;
- 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-N3) 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. © 2012 American Institute of Chemical Engineers Biotechnol. Prog.,, 2012