In cells, proteins are embedded in
a crowded environment that controls
their properties via manifold avenues including weak protein–macromolecule
interactions. A molecular level understanding of these quinary interactions
and their contribution to protein stability, function, and localization
in the cell is central to modern structural biology. Using a mutational
analysis to quantify the energetic contributions of single amino acids
to the stability of the ALS related protein superoxide dismutase I
(SOD1) in mammalian cells, we show that quinary interactions destabilize
SOD1 by a similar energetic offset for most of the mutants, but there
are notable exceptions: Mutants that alter its surface properties
can even lead to a stabilization of the protein in the cell as compared
to the test tube. In conclusion, quinary interactions can amplify
and even reverse the mutational response of proteins, being a key
aspect in pathogenic protein misfolding and aggregation.
Dendritic
polyglycerol (PG) was covalently coupled to 2-hydroxyethyl
methacrylate (HEMA) by an anionically catalyzed ring-opening polymerization
generating a dendritic PG-HEMA with four PG repetition units (PG4MA). Coatings of the methacrylate monomer were prepared by
grafting-through and compared against commercially available hydrophilic
monomers of HEMA, poly(ethylene) glycol methacrylate (PEGMA), and
poly(propylene) glycol methacrylate (PPGMA). The obtained coatings
were characterized by modern surface analytical techniques, including
water contact angle goniometry (sessile and captive bubble), attenuated
total internal reflection Fourier transform infrared spectroscopy,
and atomic force microscopy. The antifouling (AF) and fouling-release
(FR) properties of the coatings were tested against the model organisms Cobetia marina and Navicula perminuta in laboratory-scale dynamic accumulation assays as well as in a
dynamic short-term field exposure (DSFE) in the marine environment.
In addition, the hydration of the coatings and their susceptibility
toward silt uptake were evaluated, revealing a strong correlation
between water uptake, silt incorporation, and field assay performance.
While all glycol derivatives showed good resistance in laboratory
settlement experiments, PPGMA turned out to be less susceptible to
silt incorporation and outperformed PEGMA and PG4MA in
the DSFE assay.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.