albumin - publications

Predict more albumin - ligand interactions now!

1. J Biol Chem. 2012 May 1. [Epub ahead of print]

Serum albumin prevents protein aggregation and amyloid formation and retains
chaperone-like activity in the presence of physiological ligands.

Finn TE, Nunez AC, Sunde M, Easterbrook-Smith SB.

University of Sydney, Australia.

While serum albumin has an established function as a transport protein, evidence
is emerging that serum albumin may also have a role as a molecular chaperone.
Using established techniques to characterise chaperone interactions, this study
demonstrates that bovine serum albumin: 1) preferentially binds stressed over
unstressed client proteins; 2) forms stable, soluble, high molecular weight
complexes with stressed client proteins; 3) reduces the aggregation of client
proteins when it is present at physiological levels; and 4) inhibits amyloid
formation by both WT and L55P transthyretin. While the anti-aggregatory effect of
serum albumin is maintained in the presence of physiological levels of Ca2+ and
Cu2+, the presence of free fatty acids significantly alters this activity:
stabilising serum albumin at normal levels, but diminishing chaperone-like
activity at high concentrations. Moreover, here it is shown that depletion of
albumin from human plasma leads to a significant increase in aggregation under
physiologically relevant heat and shear stresses. This study demonstrates that
serum albumin possesses chaperone-like properties, and that this activity is
maintained under a number of physiologically-relevant conditions.

PMID: 22549788 [PubMed - as supplied by publisher]