Zhuravleva Irina L, Bezrodnykh Evgeniya A, Berezin Boris B, Tikhonov Vladimir E, Antonov Yurij A
N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 119334, Russia.
A. N. Nesmeyanov Institute of Organoelement Compounds, Russian Academy of Sciences, Moscow, 119334, Russia.
Macromol Biosci. 2023 Oct;23(10):e2300088. doi: 10.1002/mabi.202300088. Epub 2023 Jun 13.
Phase analysis, spectroscopic, and light scattering methods are applied to investigate the peculiarities of the interaction of oligochitosan (OCHI) with native and preheated bovine serum albumin (BSA) as well as the conformational and structural changes of BSA in BSA/OCHI complex. As shown, untreated BSA binds with OCHI mainly forming soluble electrostatic nanocomplexes, with the binding causing an increase in BSA helicity without a change in the local tertiary structure and thermal stability of BSA. In contrast, soft preheating at 56 °C enhances the complexation of BSA with OCHI and slightly destabilizes the secondary and local tertiary structures of BSA within the complex particles. Preheating at 64 °C (below the irreversible stage of BSA thermodenaturation) leads to further enhancement in the complexation and formation of insoluble complexes stabilized by both Coulomb forces and hydrophobic interactions. The finding can be promising for the preparation of biodegradable BSA/chitosan-based drug delivery systems.
