Reversible, High-Affinity Surface Capturing of Proteins Directed by Supramolecular Assembly

Area of Science:

• Biochemistry
• Materials Science
• Surface Chemistry

Background:

• Designing surfaces with controllable protein binding is crucial for biochemical and biomedical applications.
• Existing methods often lack reversibility or high affinity.

Purpose of the Study:

• To develop a dynamic supramolecular strategy for reversible protein assembly on surfaces.
• To create advanced bioanalytic and biosensor technologies using this approach.

Main Methods:

• Fabrication of a β-cyclodextrin host-derived self-assembled monolayer (β-CD-SAM) on gold.
• Utilizing multivalent host-guest interactions between β-CD-SAM and hydrophobic amino acids on proteins.
• Employing Surface Plasmon Resonance and Time-of-Flight Secondary Ion Mass Spectrometry for analysis.

Main Results:

• Demonstrated specific, high-affinity binding of model proteins (cytochrome c, insulin, α-chymotrypsin, RNase A) to β-CD-SAM.
• Achieved dissociation constants in the high nanomolar to single-digit micromolar range.
• Showcased mild conditions for efficient protein release from the surface.

Conclusions:

• The supramolecular strategy offers precise control over protein immobilization.
• This method provides a versatile platform for developing advanced bioanalytic and biosensor technologies.
• Reversible, high-affinity protein binding sites are achievable through dynamic host-guest chemistry.