Biophysical and in silico studies on the interaction of polypyridyl ruthenium complexes with human serum albumin: Overcoming low affinity and high luminescence challenges.
기술보고
1/5 보강
The concentration of free drug available for target binding is significantly influenced by its interaction with plasma proteins, primarily human serum albumin (HSA).
APA
Poznańska A, Gajda-Morszewski P, et al. (2026). Biophysical and in silico studies on the interaction of polypyridyl ruthenium complexes with human serum albumin: Overcoming low affinity and high luminescence challenges.. Journal of inorganic biochemistry, 275, 113140. https://doi.org/10.1016/j.jinorgbio.2025.113140
MLA
Poznańska A, et al.. "Biophysical and in silico studies on the interaction of polypyridyl ruthenium complexes with human serum albumin: Overcoming low affinity and high luminescence challenges.." Journal of inorganic biochemistry, vol. 275, 2026, pp. 113140.
PMID
41223740 ↗
Abstract 한글 요약
The concentration of free drug available for target binding is significantly influenced by its interaction with plasma proteins, primarily human serum albumin (HSA). In this study, we focused on the interactions between HSA and polypyridyl ruthenium complexes, a class of compounds known for their cytotoxic and antimetastatic properties. Since the fluorescence quenching technique for determining dissociation constants was not applicable in the studied case, a novel TRIC (temperature-related intensity change) technique was employed in combination with molecular docking to gain a deeper understanding of mutual recognition and binding. To assess the biological relevance of these interactions, we also conducted in vitro experiments, evaluating cytotoxicity and cellular uptake. Our findings revealed moderate binding (dissociation constant ranging from 0.2 to 1.2 mM) of the ruthenium complexes to HSA, resulting in a low protein-bound fraction. The result was consistent with the negligible impact of HSA observed on cytotoxicity and cellular uptake in human breast cancer MCF-7 cells. The integration of TRIC with molecular docking provided a valuable insight into metal complex-protein interaction and demonstrated a powerful strategy in medicinal chemistry, enabling the rational modulation of drug-protein interactions to optimize the pharmacokinetics of metal-based therapeutics.
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