Altering the Peptide Binding Selectivity of Polymeric Reverse Micelle Assemblies via Metal Ion Loading

Area of Science:

• Supramolecular chemistry
• Materials science
• Biochemistry

Background:

• Amphiphilic copolymers form supramolecular reverse micelle assemblies for selective molecular encapsulation.
• Modifying binding selectivity typically requires synthesizing new functional groups.

Purpose of the Study:

• To demonstrate that adding Zr(IV) ions to phosphonate-functionalized reverse micelles can alter their binding selectivity.
• To show that tuning phosphonate group fractions further refines selectivity.
• To develop optimized reverse micelle materials for selective phosphorylated peptide binding and enrichment.

Main Methods:

• Formation of supramolecular reverse micelle assemblies using amphiphilic copolymers with phosphonate functional groups.
• Addition of Zr(IV) ions to the interior of the reverse micelles.
• Varying the fractions of phosphonate groups in the copolymer structure.
• Testing the binding and transfer selectivity of the modified assemblies for phosphorylated peptides under various pH conditions.

Main Results:

• Zr(IV) ion addition transformed phosphonate-functionalized reverse micelles from binding positively charged peptides to binding phosphorylated peptides.
• Varying phosphonate group fractions allowed for further tuning of binding selectivity.
• Optimized materials demonstrated selective transfer and binding of phosphorylated peptides from aqueous solutions across a wide pH range.
• The materials successfully enriched phosphorylated peptides from complex mixtures.

Conclusions:

• Supramolecular reverse micelle assemblies can be dynamically tuned for selective peptide binding through ion incorporation.
• Zr(IV) ion incorporation offers a facile method to switch selectivity towards phosphorylated peptides.
• These tunable materials show promise for selective peptide enrichment in complex biological samples.