albumin - publications

Predict more albumin - ligand interactions now!


1. Biotechnol Prog. 2012 Jan 24. doi: 10.1002/btpr.1526. [Epub ahead of print]

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

Li XY, Li TH, Guo JS, Wei Y, Jing XB, Chen XS, Huang YB.

State Key Laboratory of Polymer Physics and Chemistry, Changchun Institute of
Applied Chemistry, Chinese Academy of Sciences, Changchun 130022, P. R. China.

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 2 PEG chains conjugated onto each BSA molecule as determined by MALDI-TOF
analysis. The intrinsic nonspecific binding ability of BSA was employed 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 (CD) 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.

Copyright © 2012 American Institute of Chemical Engineers (AIChE).

PMID: 22275125 [PubMed - as supplied by publisher]