showing 3 related works from this author
Tunable dynamic hydrophobic attachment of guest molecules in amphiphilic core–shell polymers
2016
In this study, synthesis and dynamic properties of amphiphilic core–shell polymers are reported as monitored through their interaction with small amphiphilic molecules. Brush-like structures are formed with a hydrophobic core surrounded by a hydrophilic shell utilizing controlled radical addition–fragmentation chain transfer (RAFT) polymerization of macromonomers consisting of linear polyglycerol chains attached to alkylene methacrylate. Continuous wave electron paramagnetic resonance (CW EPR) spectroscopy is employed to study how the amphiphilic, paramagnetic spin probe 16-DSA (16-doxyl stearic acid) interacts with polymers of different alkylene chain lengths in their hydrophobic cores and…
Ligand-Binding Cooperativity Effects in Polymer-Protein Conjugation.
2019
We present an electron paramagnetic resonance (EPR) spectroscopic characterization of structural and dynamic effects that stem from post-translational modifications of bovine serum albumin (BSA), an established model system for polymer-protein conjugation. Beyond the typical drug delivery and biocompatibility aspect of such systems, we illustrate the causes that alter internal dynamics and therefore functionality in terms of ligand-binding to the BSA protein core. Uptake of the paramagnetic fatty acid derivative 16-doxyl stearic acid by several BSA-based squaric acid macroinitiators and polymer-protein conjugates was studied by EPR spectroscopy, aided by dynamic light scattering (DLS) and z…
Evidence for Water-Tuned Structural Differences in Proteins: An Approach Emphasizing Variations in Local Hydrophilicity
2012
We present experimental evidence for the significant effect that water can have on the functional structure of proteins in solution. Human (HSA) and Bovine Serum Albumin (BSA) have an amino acid sequence identity of 75.52% and are chosen as model proteins. We employ EPR-based nanoscale distance measurements using double electron-electron resonance (DEER) spectroscopy and both albumins loaded with long chain fatty acids (FAs) in solution to globally (yet indirectly) characterize the tertiary protein structures from the bound ligands' points of view. The complete primary structures and crystal structures of HSA and as of recently also BSA are available. We complement the picture as we have re…