Human serum albumin (HSA) is the most abundant
protein in human serum. The circulation half-life of this
stable protein is extremely long (over three weeks), a feature
which has been exploited to obtain in vivo stabilization of
Using a serum albumin binding domain (ABD) derived from streptococcal
protein G as fusion partner for proteins of therapeutic value,
a strategy for production of engineered biotherapeutics with
increased in vivo stability have been developed. The serum
albumin binding activity of the ABD fusion partner results,
after injection into the blood stream, in the formation of
long-lived complexes with HSA.
|Nygren, P.-Å., Flodby,
P., Andersson, R., Wigzell, H. and Uhlén, M. 
“In vivo stabilization of a human recombinant CD4
derivative by fusion to a serum-albumin-binding receptor”
Vaccines 91, Cold Spring Harbor Laboratory. 363-368.
|Makrides, S., Nygren, P.-Å., Andrews,
B., Ford, P., Evans, K.S., Hayman, E.G., Adari, H., Levin,
J., Uhlén, M. and Toth, C.A. (1996) "Extended
in vivo half-life of human soluble complement receptor type
I fused to serum albumin-binding receptor" J. Pharm.
Exp. Therap. 277, 534-541.