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Volume 30
Issue 17
10.3390/molecules30173558
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This is an early access version, the complete PDF, HTML, and XML versions will be available soon.
Article

Electric Field-Driven Modulation of Nanomechanical Interactions Between Tyrosine Kinase Inhibitors and Human Serum Albumin: Insights from AFM-Based Force Spectroscopy

by
Yuna Fu
,
Jianhua Wang
*,
Di Gu
and
Letian Zhang
Key Laboratory of Biorheological Science and Technology, Ministry of Education, College of Bioengineering, Chongqing University, Chongqing 400044, China
*
Author to whom correspondence should be addressed.
Molecules 2025, 30(17), 3558; https://doi.org/10.3390/molecules30173558 (registering DOI)
Submission received: 22 July 2025 / Revised: 28 August 2025 / Accepted: 29 August 2025 / Published: 30 August 2025
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Abstract

Electric fields are emerging as powerful tools to actively regulate biomolecular interactions at biointerfaces. In this study, we investigated how varying electric field strengths (0–100 mV/mm) influence the interfacial interaction between human serum albumin (HSA) and six tyrosine kinase inhibitors (TKIs): imatinib, bosutinib, dasatinib, nilotinib, ponatinib, and radotinib. Using atomic force microscopy (AFM), we quantified changes in adhesion force, specific (Fi) and non-specific (F0) force, friction behavior, and protein morphology. Increasing field strength led to significant reductions in adhesion force (22–47%), Fi (27–44%), F0 (38–53%), friction force (38–67%) and constant-load friction force (43–54%), along with decreased protein average surface height and roughness, indicating electric field-induced molecular compaction and interface smoothing. Notably, more hydrophobic TKIs showed greater responsiveness. These findings highlight the potential of electric fields to modulate protein–drug interactions in a controllable manner, offering a new strategy for the development of electrically tunable drug delivery systems and smart biomedical interfaces.
Keywords: electric field; HSA; tyrosine kinase inhibitors; AFM; interaction electric field; HSA; tyrosine kinase inhibitors; AFM; interaction
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MDPI and ACS Style

Fu, Y.; Wang, J.; Gu, D.; Zhang, L. Electric Field-Driven Modulation of Nanomechanical Interactions Between Tyrosine Kinase Inhibitors and Human Serum Albumin: Insights from AFM-Based Force Spectroscopy. Molecules 2025, 30, 3558. https://doi.org/10.3390/molecules30173558

AMA Style

Fu Y, Wang J, Gu D, Zhang L. Electric Field-Driven Modulation of Nanomechanical Interactions Between Tyrosine Kinase Inhibitors and Human Serum Albumin: Insights from AFM-Based Force Spectroscopy. Molecules. 2025; 30(17):3558. https://doi.org/10.3390/molecules30173558

Chicago/Turabian Style

Fu, Yuna, Jianhua Wang, Di Gu, and Letian Zhang. 2025. "Electric Field-Driven Modulation of Nanomechanical Interactions Between Tyrosine Kinase Inhibitors and Human Serum Albumin: Insights from AFM-Based Force Spectroscopy" Molecules 30, no. 17: 3558. https://doi.org/10.3390/molecules30173558

APA Style

Fu, Y., Wang, J., Gu, D., & Zhang, L. (2025). Electric Field-Driven Modulation of Nanomechanical Interactions Between Tyrosine Kinase Inhibitors and Human Serum Albumin: Insights from AFM-Based Force Spectroscopy. Molecules, 30(17), 3558. https://doi.org/10.3390/molecules30173558

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