BC-75 Investigating the Effects of Chaotropic Salts on Protein Corona Formation in Polyethylene (PEG)-b-polylactic acid (PLA) Polymersomes
SCURS Disciplines
Biochemistry
Document Type
Poster Presentation
Abstract
In recent years, polymersomes (PS) have emerged as highly promising drug delivery systems due to their tunable membrane properties, high colloidal stability, and ability to encapsulate both hydrophilic and hydrophobic drugs. These nanoscale vesicles, composed of bilayer membranes formed by self-assembling amphiphilic copolymers, offer a unique platform for versatile therapeutic applications. However, despite their potential, a significant barrier to their clinical use is the formation of the protein corona—a layer of proteins that adsorbs onto the surface of nanoparticles upon exposure to biological fluids.
The composition of the protein corona plays a critical role in determining the PS interactions with biological systems, including circulation time, cellular uptake, and biodistribution. However, it is highly dynamic and influenced by factors such as the PS size, surface properties, and incubation conditions. Protein adsorption on the PS surface is inevitable, and due to its large impact on biological fate, researchers have begun to explore methods to engineer and control the protein corona to optimize therapeutic efficacy.
In this study, we investigate the effects of various ionic environments on the protein corona composition of PEG-b-PLA PS in bovine and human serum. Specifically, we have used chaotropic salts Na+> Ca2+> Mg2+ in order of Hofmeister Series strength to enable specific protein binding. We have identified that incubation with divalent chaotropic cations leads to significant changes in the protein corona composition, identified through mass spectroscopy. Specifically, we see a decrease in albumin adsorption and an increase in novel proteins within the corona. Particularly, the addition of Ca2+ dramatically changes the top 20 most abundant proteins due to the prevalence of calcium-binding proteins in serum. Early work using human serum indicates similar findings. By systematically analyzing how ionic strength and composition influence corona formation, we aim to identify key parameters for tailoring protein-nanoparticle interactions. This work not only advances fundamental knowledge of corona dynamics but also lays the groundwork for designing polymersomes that can be customized for individual patients.
Keywords
Nanotechnology, protein corona, drug delivery
Start Date
11-4-2025 9:30 AM
Location
University Readiness Center Greatroom
End Date
11-4-2025 11:30 AM
BC-75 Investigating the Effects of Chaotropic Salts on Protein Corona Formation in Polyethylene (PEG)-b-polylactic acid (PLA) Polymersomes
University Readiness Center Greatroom
In recent years, polymersomes (PS) have emerged as highly promising drug delivery systems due to their tunable membrane properties, high colloidal stability, and ability to encapsulate both hydrophilic and hydrophobic drugs. These nanoscale vesicles, composed of bilayer membranes formed by self-assembling amphiphilic copolymers, offer a unique platform for versatile therapeutic applications. However, despite their potential, a significant barrier to their clinical use is the formation of the protein corona—a layer of proteins that adsorbs onto the surface of nanoparticles upon exposure to biological fluids.
The composition of the protein corona plays a critical role in determining the PS interactions with biological systems, including circulation time, cellular uptake, and biodistribution. However, it is highly dynamic and influenced by factors such as the PS size, surface properties, and incubation conditions. Protein adsorption on the PS surface is inevitable, and due to its large impact on biological fate, researchers have begun to explore methods to engineer and control the protein corona to optimize therapeutic efficacy.
In this study, we investigate the effects of various ionic environments on the protein corona composition of PEG-b-PLA PS in bovine and human serum. Specifically, we have used chaotropic salts Na+> Ca2+> Mg2+ in order of Hofmeister Series strength to enable specific protein binding. We have identified that incubation with divalent chaotropic cations leads to significant changes in the protein corona composition, identified through mass spectroscopy. Specifically, we see a decrease in albumin adsorption and an increase in novel proteins within the corona. Particularly, the addition of Ca2+ dramatically changes the top 20 most abundant proteins due to the prevalence of calcium-binding proteins in serum. Early work using human serum indicates similar findings. By systematically analyzing how ionic strength and composition influence corona formation, we aim to identify key parameters for tailoring protein-nanoparticle interactions. This work not only advances fundamental knowledge of corona dynamics but also lays the groundwork for designing polymersomes that can be customized for individual patients.