Study on the interaction between oxolinic acid aggregates and protein and its analytical application

Area of Science:

• Analytical Chemistry
• Biochemistry
• Materials Science

Background:

• Oxolinic acid (OA) exhibits self-assembly properties in aqueous solutions.
• Fluorescence-based detection methods are crucial for sensitive biomolecule quantification.

Purpose of the Study:

• To develop a novel fluorescence probe based on OA aggregates for protein analysis.
• To establish a quantitative method for determining bovine serum albumin (BSA) and human serum albumin (HSA).

Main Methods:

• Self-assembly of oxolinic acid (OA) into nanoparticles in Tris-HCl buffer.
• Utilizing OA nanoparticles as fluorescence probes for protein detection.
• Quantitative analysis using fluorescence quenching and spectroscopic techniques (UV-vis, RLS, TEM).

Main Results:

• OA nanoparticles were successfully synthesized and characterized.
• A linear relationship was observed between fluorescence quenching and protein concentration for BSA and HSA.
• Achieved low detection limits: 3.4x10(-9) g mL(-1) for BSA and 2.6x10(-8) g mL(-1) for HSA.
• The interaction mechanism involves the formation of a nonluminescent complex, leading to OA disaggregation and static fluorescence quenching.

Conclusions:

• OA nanoparticles serve as effective fluorescence probes for sensitive and quantitative detection of serum albumins.
• The developed method offers a reliable approach for protein analysis in biological samples.
• Understanding the interaction mechanism provides insights into the probe's behavior and enhances analytical performance.