Bovine serum albumin under the influence of alkali metal halides

The hydration shell of a protein is so important and an integral part of it, that protein's structure, stability and functionality cannot be conceived in its absence. This layer has unique properties not found in bulk water. However, ions, always present in the protein environment, disturb the...

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Bibliographic Details
Published in:RSC advances 2025-01, Vol.15 (1), p.244-251
Main Authors: Carreón, Yojana J P, Jaramillo-Granada, A M, Fuentes-López, D, Reyes-Figueroa, A D, González-Gutiérrez, J, Mercado-Uribe, H
Format: Article
Language:English
Subjects:
Alkali metals
Cattle
Chemistry
Fourier transforms
Halides
Hydration
Image analysis
Infrared analysis
Infrared imagery
Infrared signatures
Lithium
Metal halides
Photon correlation spectroscopy
Proteins
Serum albumin
Shell stability
Thermogravimetry
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Summary:The hydration shell of a protein is so important and an integral part of it, that protein's structure, stability and functionality cannot be conceived in its absence. This layer has unique properties not found in bulk water. However, ions, always present in the protein environment, disturb the hydration shell depending on their nature and concentration. In this work, we study the effect of four alkali metal halides (LiCl, NaCl, KCl and CsCl) on a Bovine Serum Albumin (BSA) suspension. In order to investigate the influence of such ions on this protein, we use several experimental methods: dynamic light scattering, differential scanning calorimetry, thermogravimetry, Fourier transform infrared spectroscopy and image analysis. We found that Li and Na prevent protein aggregation. Moreover, the ion size affects the interaction with the secondary structure of the protein (Amide III band). Notably, for the smallest ion (Li ), the water-ion interaction dominates over the Amide A band signature, contrasting with the other ions. We also differentiate between bulk and hydration water through the evaporation of protein suspensions.
ISSN:2046-2069
2046-2069
DOI:10.1039/d4ra04503c