Electrostatic assisted fabrication and dissociation of multi-component proteinosomes

Cai, Yaqian; Yu, Qianyu; Zhao, Hanying

doi:10.1016/j.jcis.2020.05.013

Cited by 11 publications

(9 citation statements)

References 58 publications

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“…The formation of polymer particles is caused by the phase transition of PNIPAAm, forming the hydrophobic core surrounded by BSA shell. Other literatures also suggested that protein-PNIPAAm conjugates form stable aggregates above the LCST [ 14 , 20 , 28 , 30 , 31 ]. Of particular interest is that the conjugates with less than 2-mole equivalents of CTA did not form the aggregate plausibly due to the insufficient amount of introduced PNIPAAm.…”

Section: Resultsmentioning

confidence: 98%

“…GF approach uses functionalized proteins as initiation sites from where monomers are polymerized through living radical polymerization in an aqueous solution. However, only few reports have investigated the introduction of PNIPAAm into proteins through reversible addition-fragmentation chain transfer (RAFT) polymerization [ 24 , 25 , 26 , 27 , 28 ]. These reports confirmed the successful living radical polymerization of NIPAAm from proteins and the retained activity of protein-polymer conjugates after PNIPAAm introduction.…”

Section: Introductionmentioning

confidence: 99%

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Temperature Responsive Polymer Conjugate Prepared by “Grafting from” Proteins toward the Adsorption and Removal of Uremic Toxin

et al. 2022

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In this study, temperature-responsive polymer-protein conjugate was synthesized using a “grafting from” concept by introducing a chain transfer agent (CTA) into bovine serum albumin (BSA). The BSA-CTA was used as a starting point for poly(N-isopropylacrylamide) (PNIPAAm) through reversible addition-fragmentation chain transfer polymerization. The research investigations suggest that the thermally responsive behavior of PNIPAAm was controlled by the monomer ratio to CTA, as well as the amount of CTA introduced to BSA. The study further synthesized the human serum albumin (HSA)-PNIPAAm conjugate, taking the advantage that HSA can specifically adsorb indoxyl sulfate (IS) as a uremic toxin. The HSA-PNIPAAm conjugate could capture IS and decreased the concentration by about 40% by thermal precipitation. It was also revealed that the protein activity was not impaired by the conjugation with PNIPAAm. The proposed strategy is promising in not only removal of uremic toxins but also enrichment of biomarkers for early diagnostic applications.

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Section: Resultsmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Temperature Responsive Polymer Conjugate Prepared by “Grafting from” Proteins toward the Adsorption and Removal of Uremic Toxin

et al. 2022

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“…As the zeta potential of hydrolyzing NPs decreased whereas that of the nonhydrolyzing NPs was constant, the hydrolysis of the esters from the NP surface, and subsequent neutralization of surface charge, drove the release of proteins from the nanocomposite hydrogel. Release from nonhydrolyzing NPs may be attributed to either adsorption–desorption equilibria or the ionic strength of the release medium, which can also disrupt electrostatic interactions between proteins and surfaces . Interestingly, the release of transferrin from −COOtBu NPs (30%) was slower than that from −COOEt NPs (42%) over 1 d before catching up at 3 d, matching the slower neutralization of zeta potential observed for −COOtBu NPs.…”

Section: Resultsmentioning

confidence: 77%

Protein Release by Controlled Desorption from Transiently Cationic Nanoparticles

Cheung

Xue

Kurtz

et al. 2023

ACS Appl. Mater. Interfaces

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Therapeutic release from hydrogels is traditionally controlled by encapsulation within nanoparticles; however, this strategy is limited for the release of proteins due to poor efficiency and denaturation. To overcome this problem, we designed an encapsulation-free release platform where negatively charged proteins are adsorbed to the exterior of transiently cationic nanoparticles, thus allowing the nanoparticles to be formulated separately from the proteins. Release is then governed by the change in nanoparticle surface charge from positive to neutral. To achieve this, we synthesized eight zwitterionic poly(lactide-block-carboxybetaine) copolymer derivatives and formulated them into nanoparticles with differing surface chemistry. The nanoparticles were colloidally stable and lost positive charge at rates dependent on the hydrolytic stability of their surface ester groups. The nanoparticles (NPs) were dispersed in a physically cross-linked hyaluronan-based hydrogel with one of three negatively charged proteins (transferrin, panitumumab, or granulocyte-macrophage colony-stimulating factor) to assess their ability to control release. For all three proteins, dispersing NPs within the gels resulted in significant attenuation of release, with the extent modulated by the hydrolytic stability of the surface groups. Release was rapid from fast-hydrolyzing ester groups, reduced with slow-hydrolyzing bulky ester groups, and very slow with nonhydrolyzing amide groups. When positively charged lysozyme was loaded into the nanocomposite gel, there was no significant attenuation of release compared to gel alone. These data demonstrate that electrostatic interactions between the protein and NP are the primary driver of protein release from the hydrogel. All released proteins retained bioactivity as determined with in vitro cell assays. This release strategy shows tremendous versatility and provides a promising new platform for controlled release of anionic protein therapeutics.

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“…Electrostatic interaction-based stacked structures of viruses and polymers are considered as new 3D structures and play an important role in the research of multiple interactions such as ligand–receptor interactions. − Among them, virus–nanomaterial interactions often lead to bioactive materials such as the virus-coated nanocellulose nanofibers as artificial human tissues. Thus, we discuss the use of electrostatic interactions for the construction of virus–polymer hybrids that could apply to drug delivery such as delivery of Prussian blue or other drugs.…”

Section: Applications Of Virus or Viruslike Structuresmentioning

confidence: 99%

Virus-Based Supramolecular Structure and Materials: Concept and Prospects

Hou

Jiang

et al. 2021

ACS Appl. Bio Mater.

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Rodlike and spherelike viruses are various monodisperse nanoparticles that can display small molecules or polymers with unique distribution following chemical modifications. Because of the monodisperse property, aggregates in synthetic protein−polymer nanoparticles could be eliminated, thus improving the probability for application in protein−polymer drug. In addition, the monodisperse virus could direct the growth of metal materials or inorganic materials, finding applications in hydrogel, drug delivery, and optoelectronic and catalysis materials. Benefiting from the advantages, the virus or viruslike particles have been widely explored in the field of supramolecular chemistry. In this review, we describe the modification and application of virus and viruslike particles in surpramolecular structures and biomedical research.

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Electrostatic assisted fabrication and dissociation of multi-component proteinosomes

Cited by 11 publications

References 58 publications

Temperature Responsive Polymer Conjugate Prepared by “Grafting from” Proteins toward the Adsorption and Removal of Uremic Toxin

Temperature Responsive Polymer Conjugate Prepared by “Grafting from” Proteins toward the Adsorption and Removal of Uremic Toxin

Protein Release by Controlled Desorption from Transiently Cationic Nanoparticles

Virus-Based Supramolecular Structure and Materials: Concept and Prospects

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