High-resolution AFM imaging of the CA125 protein and its aptamer-based complexes

Area of Science:

• Biomolecular interactions
• Nanotechnology applications
• Medical diagnostics

Background:

• Aptamer/antigen complexation is crucial for medical diagnostic systems.
• Accurate evaluation of complex formation is needed to improve diagnostic reliability.
• Current methods may not fully capture the efficiency of these specific binding events.

Purpose of the Study:

• To propose a novel approach for evaluating aptamer/antigen complexation efficiency.
• To utilize high-resolution AFM imaging data for quantitative assessment.
• To demonstrate the method's applicability with specific antigen variants and aptamers.

Main Methods:

• High-resolution Atomic Force Microscopy (AFM) imaging.
• Quantitative analysis of sorbed object height and volume on mica surfaces.
• Complexation studies involving CA125 antigen variants (seven or one SEA domain) and aptamers.

Main Results:

• The study successfully demonstrates an approach to evaluate aptamer/antigen complexation efficiency using AFM.
• Comprehensive analysis of height and volume provides a reliable measure of complex formation success.
• The method's applicability is confirmed with different CA125 antigen constructs and aptamers.

Conclusions:

• AFM-based analysis of height and volume offers a robust method for assessing aptamer/antigen complexation.
• This approach can enhance the development of more efficient and reliable diagnostic systems.
• The findings contribute to the field of aptamer-based biosensing and molecular recognition.