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Peer-reviewedCC BY-NC-ND 4.0ACS Omega

Comparative Analysis of the Binding Characteristics of Fluorescein and Rhodamine B with Bovine Serum Albumin

  • Samson Olusegun Afolabi1
  • Viktoria A. Feoktistova1
  • Dmitrii Sbytov1
  • Oleg Novikov1
  • Anna Botnar1
  • Sviatlana Ulasevich1
  • Ekaterina V. Skorb1
  • Sergey Shityakov1,2
  1. 1ITMO University , , Lomonosova St. 9 , ,
  2. 2Sechenov First Moscow State Medical University (Sechenov University) , , ,
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Abstract

Bovine serum albumin (BSA) serves as a key model for investigating protein–ligand interactions and is crucial for understanding drug pharmacokinetics and developing biomedical probes. This study presents a comprehensive comparative analysis of the binding of fluorescein and rhodamine B to BSA, employing UV–vis absorption, fluorescence, molecular docking, and 1000 ns molecular dynamics (MD) simulations. The results revealed competitive binding, with rhodamine B exhibiting a greater affinity (ΔGMMGBSA = −48.17 kcal/mol) than fluorescein (−23.16 kcal/mol), which was supported by fluorescence quenching and binding analyses. Molecular docking confirmed Sudlow’s site I as the primary binding site, whereas MD simulations highlighted stable complexes driven by van der Waals and electrostatic forces, particularly for rhodamine B. Unexpectedly, the superior affinity of rhodamine B under physiological pH deviates from lipophilic trends. These findings enhance the molecular understanding of dye–protein interactions, providing a robust basis for designing advanced fluorescent probes, drug conjugates, and diagnostic platforms.

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Cite

BibTeXRIS
BibTeX
@article{afolabi2026comparative,
  title = {{Comparative Analysis of the Binding Characteristics of Fluorescein and Rhodamine B with Bovine Serum Albumin}},
  author = {Samson Olusegun Afolabi and Viktoria A. Feoktistova and Dmitrii Sbytov and Oleg Novikov and Anna Botnar and Sviatlana Ulasevich and Ekaterina V. Skorb and Sergey Shityakov},
  journal = {ACS Omega},
  year = {2026},
  month = oct,
  doi = {10.1021/acsomega.5c12646},
  url = {https://pubs.acs.org/acsodf/article/11/42/64388/5450245/Comparative-Analysis-of-the-Binding},
  note = {CC BY-NC-ND 4.0},
}
RIS
TY  - JOUR
TI  - Comparative Analysis of the Binding Characteristics of Fluorescein and Rhodamine B with Bovine Serum Albumin
AU  - Samson Olusegun Afolabi
AU  - Viktoria A. Feoktistova
AU  - Dmitrii Sbytov
AU  - Oleg Novikov
AU  - Anna Botnar
AU  - Sviatlana Ulasevich
AU  - Ekaterina V. Skorb
AU  - Sergey Shityakov
PY  - 2026
DA  - 2026/10/13
JO  - ACS Omega
DO  - 10.1021/acsomega.5c12646
UR  - https://pubs.acs.org/acsodf/article/11/42/64388/5450245/Comparative-Analysis-of-the-Binding
AB  - Bovine serum albumin (BSA) serves as a key model for investigating protein–ligand interactions and is crucial for understanding drug pharmacokinetics and developing biomedical probes. This study presents a comprehensive comparative analysis of the binding of fluorescein and rhodamine B to BSA, employing UV–vis absorption, fluorescence, molecular docking, and 1000 ns molecular dynamics (MD) simulations. The results revealed competitive binding, with rhodamine B exhibiting a greater affinity (ΔGMMGBSA = −48.17 kcal/mol) than fluorescein (−23.16 kcal/mol), which was supported by fluorescence quenching and binding analyses. Molecular docking confirmed Sudlow’s site I as the primary binding site, whereas MD simulations highlighted stable complexes driven by van der Waals and electrostatic forces, particularly for rhodamine B. Unexpectedly, the superior affinity of rhodamine B under physiological pH deviates from lipophilic trends. These findings enhance the molecular understanding of dye–protein interactions, providing a robust basis for designing advanced fluorescent probes, drug conjugates, and diagnostic platforms.
SN  - 2470-1343
ER  -