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dc.contributor.authorMarin, Alexander
dc.contributor.authorTaraban, Marc B
dc.contributor.authorPatel, Vanshika
dc.contributor.authorYu, Y Bruce
dc.contributor.authorAndrianov, Alexander K
dc.date.accessioned2022-11-22T21:15:34Z
dc.date.available2022-11-22T21:15:34Z
dc.date.issued2022-11-01
dc.identifier.urihttp://hdl.handle.net/10713/20215
dc.description.abstractThe in vivo potency of polyphosphazene immunoadjuvants is inherently linked to the ability of these ionic macromolecules to assemble with antigenic proteins in aqueous solutions and form physiologically stable supramolecular complexes. Therefore, in-depth knowledge of interactions in this biologically relevant system is a prerequisite for a better understanding of mechanism of immunoadjuvant activity. Present study explores a self-assembly of polyphosphazene immunoadjuvant-PCPP and a model antigen-lysozyme in a physiologically relevant environment-saline solution and neutral pH. Three analytical techniques were employed to characterize reaction thermodynamics, water-solute structural organization, and supramolecular dimensions: isothermal titration calorimetry (ITC), water proton nuclear magnetic resonance (wNMR), and dynamic light scattering (DLS). The formation of lysozyme-PCPP complexes at near physiological conditions was detected by all methods and the avidity was modulated by a physical state and dimensions of the assemblies. Thermodynamic analysis revealed the dissociation constant in micromolar range and the dominance of enthalpy factor in interactions, which is in line with previously suggested model of protein charge anisotropy and small persistence length of the polymer favoring the formation of high affinity complexes. The paper reports advantageous use of wNMR method for studying protein-polymer interactions, especially for low protein-load complexes.en_US
dc.description.urihttps://doi.org/10.3390/molecules27217424en_US
dc.language.isoenen_US
dc.relation.ispartofMolecules (Basel, Switzerland)en_US
dc.subjectdynamic light scatteringen_US
dc.subjectimmunoadjuvanten_US
dc.subjectisothermal titration calorimetryen_US
dc.subjectmodel antigenen_US
dc.subjectpolyphosphazenesen_US
dc.subjectprotein–polyelectrolyte interactionsen_US
dc.subjectsupramolecular assemblyen_US
dc.subjectvaccine delivery vehicleen_US
dc.subjectwater proton transverse relaxation rateen_US
dc.titleSupramolecular Protein-Polyelectrolyte Assembly at Near Physiological Conditions-Water Proton NMR, ITC, and DLS Study.en_US
dc.typeArticleen_US
dc.identifier.doi10.3390/molecules27217424
dc.identifier.pmid36364250
dc.source.journaltitleMolecules (Basel, Switzerland)
dc.source.volume27
dc.source.issue21
dc.source.countrySwitzerland


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