A Self-Assembling Peptide Scaffold for the Multivalent Presentation of Antigens

Area of Science:

• Biotechnology
• Materials Science
• Nanotechnology

Background:

• Self-assembling peptides offer tunable platforms for multivalent ligand presentation.
• Coiled-coil structures are amenable to creating ordered, higher-order assemblies.

Purpose of the Study:

• To develop a novel fiber-forming coiled-coil peptide scaffold for simultaneous display of diverse ligands.
• To evaluate the impact of multivalent ligand presentation on binding affinity and bioassay sensitivity.

Main Methods:

• Design and synthesis of a fiber-forming coiled-coil peptide.
• Decoration of the peptide scaffold with carbohydrate (mannose, Leishmania glycotope) and peptide (diphtheria toxin epitope) ligands.
• Characterization of self-assembly and nanostructure formation.
• Binding assays with specific antibodies and carbohydrate-binding proteins.
• Evaluation in bioanalytical assays for disease biomarker detection.

Main Results:

• The peptide successfully self-assembled into nanofibers displaying multiple ligands without compromising structural integrity.
• Multivalent display significantly increased binding avidity for anti-diphtheria toxin antibodies and mannose-binding proteins.
• The scaffold demonstrated enhanced sensitivity for detecting Leishmania-specific antibodies in clinical samples (human and canine sera).

Conclusions:

• Coiled-coil peptide nanofibers provide a versatile and effective platform for multivalent ligand display.
• This self-assembly approach enhances biomolecular interactions and shows significant potential for developing sensitive diagnostic tools and bioassays.
• The technology is applicable to various ligands, including pathogen-specific epitopes, for disease detection.