albumin - publications

Predict more albumin - ligand interactions now!

1. Langmuir. 2012 May 2. [Epub ahead of print]

Fibronectin and bovine serum albumin adsorption and conformational dynamics on
inherently conducting polymers: a QCM-D study.

Molino P, Higgins MJ, Innis PC, Kapsa RM, Wallace GG.

Quartz Crystal Microbalance with Dissipation monitoring (QCM-D) was employed to
characterise the adsorption of the model proteins, Bovine serum albumin (BSA) and
Fibronectin (FN), to polypyrrole doped with dextran sulphate (PPy-DS) as a
function of DS loading and surface roughness. BSA adsorption was greater on
surfaces of increased roughness and was above what could be explained by the
increase in surface area alone. Furthermore the additional mass adsorbed on the
rough films was concomitant with an increase in the rigidity of the protein
layer. Analysis of the dynamic viscoelastic properties of the protein adlayer
reveal BSA adsorption on the rough films occurs in two phases: 1) arrival and
initial adsorption of protein to the polymer surface; and 2) post-adsorption
molecular rearrangement to a more dehydrated and compact conformation that
facilitates further recruitment of protein to the polymer interface, likely
forming a multilayer. In contrast, FN adsorption was independent of surface
roughness. However, films prepared from solutions containing the highest
concentration of DS (20mg/ml) demonstrated both an increase in adsorbed mass and
adlayer viscoelasticity. This is attributed to the higher DS loading in the
conducting polymer film resulting in presentation of a more hydrated molecular
structure indicative of a more unfolded and bioactive conformation. Modulating
the redox state of the PPy-DS polymers was shown to modify both the adsorbed mass
and viscoelastic nature of FN adlayers. An oxidising potential increased both the
total adsorbed mass and the adlayer viscoelasticity. Our findings demonstrate
that modification of polymer physicochemical and redox condition alters the
nature of protein-polymer interaction, a process that may be exploited to tailor
the bioactivity of protein through which interactions with cells and tissues may
be controlled.

PMID: 22551342 [PubMed - as supplied by publisher]