Native mass spectrometry analysis of conjugated HSA and BSA complexes with various flavonoids

Mass spectrometry was used to study the binding interaction between serum albumin proteins (BSA and HSA) and flavone dyes, which is known to induce large fluorescence signals for protein detection. By electrospray ionization mass spectrometry (ESI-MS), multiple charged species/states could be produc...

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Bibliographic Details
Published in:Analyst (London) 2024-03, Vol.149 (6), p.1929-1938
Main Authors: Alexander, Nicolas, McDonald, Lucas, Wesdemiotis, Chrys, Pang, Yi
Format: Article
Language:English
Subjects:
Ammonium acetate
Binding sites
Buffers
Chemistry
Conjugates
Dyes
Flavonoids
Mass spectrometry
Proteins
Serum albumin
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Summary:Mass spectrometry was used to study the binding interaction between serum albumin proteins (BSA and HSA) and flavone dyes, which is known to induce large fluorescence signals for protein detection. By electrospray ionization mass spectrometry (ESI-MS), multiple charged species/states could be produced in ammonium acetate buffer, while preserving the native structures of the proteins. Subsequent introduction of a flavone dye into the buffered solution resulted in an immediate interaction, forming the respective protein-dye conjugates associated by non-covalent interactions. Formation of protein-dye conjugates induced a notable response in the ESI-MS spectra, including changes in both the charge states and molecular mass of the protein species. The resulting data pointed out that the protein-flavone dye maintained a 1 : 1 ratio in the conjugate, although multiple binding sites for drug molecules are present in albumin proteins. Albumin protein has multiple binding sites for drugs. By electron-ionization mass spectrometry (ESI-MS), the albumin protein in its native conformation is shown to form an albumin-flavone complex in a 1 : 1 ratio.
ISSN:0003-2654
1364-5528
DOI:10.1039/d3an02070c