Document Type



Netropsin is an antibiotic that binds in the minor grooves of DNA, which also exhibits anticancer properties. There have been many previous studies that explored the binding of this drug to DNA using traditional methods where an ensemble averaging is used. In this study we explore the interaction of Netropsin with DNA at a single molecule level using dual beam optical tweezers. We trapped and stretched a single DNA molecule using optical tweezers to measure the force experienced by the DNA as a function of extension in the absence and presence of various concentrations of Netropsin. Our results show the binding affinity of Netropsin is in micro-molar range which corroborates with the previous studies. The preliminary data from this study proposes that melting of the DNA facilitates the binding of Netropsin. This outcome is hard to believe because melting of the DNA alters its double helix structure, which should not facilitate any groove binders. Additional experiments would allow us to better understand the binding kinetics of Netropsin and completely characterize it. Furthermore, this can serve as a base model to study drugs with similar binding properties and can assist in the development of potential therapeutics.


Biological Sciences and Physics, Photonics and Optical Engineering

Thesis Comittee

Dr. Thayaparan Paramanathan, Thesis Advisor
Dr. Kenneth Adams, Thesis Advisor
Dr. Elif Demirbas, Committee Member

Copyright and Permissions

Original document was submitted as an Honors Program requirement. Copyright is held by the author.