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<p>The growing use of vaccines based on chitosan/protein complexes requires a deep knowledge of how the structure of chitosan influences the complexation with the protein and its structural alterations and thermal stability within complexes. Herein, the effect of the overall charge of partially N-reacetylated short chain chitosan derivatives (ROCHI) on the thermodynamic properties, structure, and thermal stability of ovalbumin (OVA) and OVA/ROCHIs complexes vary in the degree of acetylation (DA 25, 31, and 40%) is described. As shown, the stoichimetric composition of ROCHI/OVA complexes, size, yield as well as their solubility change dramatically during the transition of DA from 31 to 40%. The complexation of OVA with ROCHI-40 having predominantly a hydrophobic nature intensifies with the temperature while the complexation with ROCHI-25 and ROCHI-31 has predominantly electrostatic nature. A partial irreversible destabilization or two-step reversible alterations in the OVA structure are found when ROCHI-25 or ROCHI-31 are applied, correspondingly. No alteration is observed when OVA is bound with ROCHI-40. The thermal stability of OVA in the complex remains insensitive to the presence of ROCHI of all above mentioned DA values. The results of the study open up new possibilities for creating vaccines based on OVA and chitosan.</p>

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Effect of overall charge of oligochitosan on structure and thermal stability of ovalbumin and thermodynamic properties ovalbumin/oligochitosan systems

  • 期刊论文

  • 发表日期：

    2025年4月10日

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  • Irina L. Zhuravleva,
  • Evgeniya A. Bezrodnykh,
  • Viktor N. Orlov,
  • Boris B. Berezin,
  • Vladimir E. Tikhonov,
  • Yurij A. Antonov

摘要

The growing use of vaccines based on chitosan/protein complexes requires a deep knowledge of how the structure of chitosan influences the complexation with the protein and its structural alterations and thermal stability within complexes. Herein, the effect of the overall charge of partially N-reacetylated short chain chitosan derivatives (ROCHI) on the thermodynamic properties, structure, and thermal stability of ovalbumin (OVA) and OVA/ROCHIs complexes vary in the degree of acetylation (DA 25, 31, and 40%) is described. As shown, the stoichimetric composition of ROCHI/OVA complexes, size, yield as well as their solubility change dramatically during the transition of DA from 31 to 40%. The complexation of OVA with ROCHI-40 having predominantly a hydrophobic nature intensifies with the temperature while the complexation with ROCHI-25 and ROCHI-31 has predominantly electrostatic nature. A partial irreversible destabilization or two-step reversible alterations in the OVA structure are found when ROCHI-25 or ROCHI-31 are applied, correspondingly. No alteration is observed when OVA is bound with ROCHI-40. The thermal stability of OVA in the complex remains insensitive to the presence of ROCHI of all above mentioned DA values. The results of the study open up new possibilities for creating vaccines based on OVA and chitosan.