albumin - publications

Predict more albumin - ligand interactions now!


1. Biosci Trends. 2012 Apr;6(2):81-8.

N-terminal PEGylation of human serum albumin and investigation of its
pharmacokinetics and pulmonary microvascular retention.

Zhao T, Yang Y, Zong AZ, Tan HN, Song XL, Meng S, Song CX, Pang GL, Wang FS.

Institute of Biochemical and Biotechnological Drugs, School of Pharmaceutical
Sciences, Shandong University, Ji'nan, China.

Human serum albumin (HSA) is used as an important plasma volume expander in
clinical practice. In the present study, HSA was N-terminally PEGylated and a
PEGylated HAS (PEG-HSA) carrying one chain of PEG (20 kDa) per HSA molecule was
obtained. The purity, secondary structure and hydrodynamic radius of the modified
protein were characterized using sodium dodecyl sulfate polyacrylamide gel
electrophoresis, circular dichroism measurements, and dynamic light scattering,
respectively. The pharmacokinetics in normal mice and vascular permeability of
the PEG-HSA in a lipopolysaccharide-induced acute lung injury mice model were
evaluated. The results showed that the biological half-life of the modified HSA
was approximately 2.2 times of that of native HSA, and PEG-HSA had a lower
vascular permeability which suggested that PEGylation of HSA could reduce
extravasation into interstitial space. It can be inferred that due to the
prolonged half-life time and enhanced vascular retention, the molecularly
homogeneous PEG-HSA may be a superior candidate as a plasma volume expander in
treating capillary permeability increase related illness.

PMID: 22621990 [PubMed - in process]