Protein-surface interactions in nano-scale biosensors for IL-6 detection using functional monolayers
Serena Giberti1, Sutapa Dutta1, Stefano Corni2
1Institute Nanoscience - CNR-NANO, Center S3, via G. Campi 213/A, 41125, Modena, Italy. giorgia.brancolini@nano.cnr.it.
Nanoscale
|January 20, 2025
Summary
Optimizing surfaces with mixed charged and hydrophobic ligands significantly enhances interleukin-6 (IL-6) binding affinity for improved biosensor design. This approach boosts IL-6 recognition, even in high ionic strength conditions.
Area of Science:
- Biomolecular Engineering
- Surface Chemistry
- Computational Biology
Background:
- Interleukin-6 (IL-6) is a crucial cancer biomarker.
- Developing sensitive biosensors requires understanding protein-surface interactions.
- Alkyl-functionalized surfaces are key components in biosensor technology.
Purpose of the Study:
- To investigate the interaction dynamics between IL-6 and modified surfaces.
- To guide the design of advanced biosensors for IL-6 detection.
- To optimize surface properties for enhanced protein biomarker recognition.
Main Methods:
- Multiscale simulations: classical molecular dynamics and Brownian dynamics.
- Surface modification using self-assembled monolayers (SAMs) with mixed ligands.
- Experimental validation using surface plasmon resonance (SPR) binding assays.
Main Results:
- Mixed SAMs with charged and hydrophobic ligands dramatically altered IL-6 interaction strength.
- Increased charged ligand content in SAMs enhanced IL-6 binding affinity.
- High IL-6 binding affinity was maintained under high ionic strength conditions.
- Hydrophobic and electrostatic interactions were identified as key drivers of IL-6 affinity.
Conclusions:
- Mixed SAMs offer a promising strategy for enhancing IL-6 recognition in biosensors.
- Surface composition optimization is critical for biosensing performance.
- The findings can be extended to improve detection of other protein biomarkers.
