  Prevention of protein aggregation and thus stabilization of proteins has
large biological and biotechnological implications. Here, we show that
inhibition of amyloid-like aggregates is possible in stoichiometric conjugates
of polymer surfactant and bovine serum albumin (BSA) chosen as a model protein.
We investigate using a combination of Thioflavin-T fluorescence spectroscopy,
dynamic light scattering and FTIR spectroscopy the aggregation behavior in
polymer surfactant modified and unmodified (native) BSA solutions. The
BSA-polymer surfactant conjugates are stable up to 5 days under aggregation
conditions, while native BSA forms amyloid fibrillar structures. Further,
DLS-based micro-rheology studies performed with heat-treated 100 to 200 {\mu}M
native BSA aggregates provided understanding of the equilibrium elastic and
viscous moduli over a very large frequency range, reaching MHz, which are
inaccessible using bulk rheology. Our results indicate that after 6 days of
aggregation conditions, elastic moduli showed values between 1.2 to 3.6 Pa
corresponding to an entanglement length ({\xi}) of 105 nm. Interestingly,
heating 200 {\mu}M native BSA solution at 65 degree C for 2 days in a plastic
Eppendorf resulted in self-standing films. These films exhibited strong
ThT-fluorescence intensity and a predominant \b{eta}-sheet secondary structure
from the FTIR studies, suggesting that self-standing microstructure resulted
from hierarchical self-assembly of amyloid fibrils.
