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Full-Text Articles in Engineering
Designing Electrostatic Interactions Via Polyelectrolyte Monomer Sequence, Tyler K. Lytle, Li-Wei Chang, Natalia Markiewicz, Sarah L. Perry, Charles E. Sing
Designing Electrostatic Interactions Via Polyelectrolyte Monomer Sequence, Tyler K. Lytle, Li-Wei Chang, Natalia Markiewicz, Sarah L. Perry, Charles E. Sing
Chemical Engineering Faculty Publication Series
Charged polymers are ubiquitous in biological systems because electrostatic interactions can drive complicated structure formation and respond to environmental parameters such as ionic strength and pH. In these systems, function emerges from sophisticated molecular design; for example, intrinsically disordered proteins leverage specific sequences of monomeric charges to control the formation and function of intracellular compartments known as membraneless organelles. The role of a charged monomer sequence in dictating the strength of electrostatic interactions remains poorly understood despite extensive evidence that sequence is a powerful tool biology uses to tune soft materials. In this article, we use a combination of theory, …
Design Rules For Encapsulating Proteins Into Complex Coacervates, Whitney Blocher Mctigue, Sarah L. Perry
Design Rules For Encapsulating Proteins Into Complex Coacervates, Whitney Blocher Mctigue, Sarah L. Perry
Chemical Engineering Faculty Publication Series
We investigated the encapsulation of the model proteins bovine serum albumin (BSA), human hemoglobin (Hb), and hen egg white lysozyme (HEWL) into two-polymer complex coacervates as a function of polymer and solution conditions. Electrostatic parameters such as pH, protein net charge, salt concentration, and polymer charge density can be used to modulate protein uptake. While the use of a two-polymer coacervation system enables the encapsulation of weakly charged proteins that would otherwise require chemical modification to facilitate electrostatic complexation, we observed significantly higher uptake for proteins whose structure includes a cluster of like-charged residues on the protein surface. In addition …