Structure-affinity correlations and separable optical activity in carbon nanotube protein coronas

Area of Science:

• Nanomaterials Science
• Biomolecular Engineering
• Analytical Chemistry

Background:

• The biomolecular corona on nanoparticles alters their biological identity.
• Single-walled carbon nanotubes (SWCNTs) offer tunable surfaces and fluorescence for studying corona formation.
• Understanding SWCNT surface chemistry's impact on corona and fluorescence is crucial.

Purpose of the Study:

• To investigate how SWCNT surface chemistry influences protein corona composition.
• To correlate protein corona profiles with SWCNT near-infrared fluorescence.
• To elucidate design principles for SWCNT-based sensors and biomarker platforms.

Main Methods:

• Synthesized and characterized a library of 25 chemically modified SWCNTs.
• Quantified protein enrichment using quantitative proteomics.
• Measured fluorescence response using near-infrared fluorescence spectroscopy.

Main Results:

• Polymer and quantum-defect chemistry independently modulated corona composition.
• Dispersion forces were identified as the primary driver of protein-nanotube binding.
• Protein enrichment and fluorescence response were partially decoupled, with enriched proteins showing responses at lower concentrations.

Conclusions:

• SWCNT surface chemistry dictates protein corona assembly.
• Dispersion forces play a universal role in protein-nanotube interactions.
• Decoupled enrichment and fluorescence responses offer insights for optimizing SWCNT sensor performance and biomarker discovery.