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- Title
PEGylation of bovine serum albumin using click chemistry for the application as drug carriers.
- Authors
Li, Xiao-Yuan; Li, Tai-Hang; Guo, Jin-Shan; Wei, Ying; Jing, Xia-Bin; Chen, Xue-Si; Huang, Yu-Bin
- 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
- Subjects
SERUM albumin; CLICK chemistry; DRUG carriers; POLYETHYLENE glycol; CONJUGATED polymers; RING formation (Chemistry); MOLECULAR structure; ENZYME activation
- Publication
Biotechnology Progress, 2012, Vol 28, Issue 3, p856
- ISSN
8756-7938
- Publication type
Article
- DOI
10.1002/btpr.1526