Predicting Protein–Polymer Block CopolymerSelf-Assembly from Protein Properties
2019
Protein–polymer
bioconjugate self-assembly has attracted
a great deal of attention as a method to fabricate protein nanomaterials
in solution and the solid state. To identify protein properties that
affect phase behavior in protein–polymer block copolymers,
a library of 15 unique protein-b-poly(N-isopropylacrylamide) (PNIPAM) copolymers comprising 11 different
proteins was compiled and analyzed. Many attributes of phase behavior
are found to be similar among all studied bioconjugates regardless
of protein properties, such as formation of micellar phases at high
temperature and low concentration, lamellar ordering with increasing
temperature, and disordering at high concentration, but several key
protein-dependent trends are also observed. In particular, hexagonal
phases are only observed for proteins within the molar mass range
20–36 kDa, where ordering quality is also significantly enhanced.
While ordering is generally found to improve with increasing molecular
weight outside of this range, most large bioconjugates exhibited weaker
than predicted assembly, which is attributed to chain entanglement
with increasing polymer molecular weight. Additionally, order–disorder
transition boundaries are found to be largely uncorrelated to protein
size and quality of ordering. However, the primary finding is that
bioconjugate ordering can be accurately predicted using only protein
molecular weight and percentage of residues contained within β
sheets. This model provides a basis for designing protein–PNIPAM
bioconjugates that exhibit well-defined self-assembly and a modeling
framework that can generalize to other bioconjugate chemistries.
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