Exploiting Materials Binding Peptides for the Organization of Resilient Biomolecular Constructs

Area of Science:

• Biomaterials Science
• Protein Engineering
• Surface Chemistry

Background:

• Natural resilin protein provides exceptional mechanical resilience due to its unique structure and cross-linking mechanisms.
• Replicating resilin's properties in synthetic materials has been challenging, potentially due to difficulties in achieving natural preorganization for cross-linking.

Purpose of the Study:

• To engineer resilin-like peptides (RLPs) conjugated with a graphene-binding peptide (P1) to create P1/RLP conjugates.
• To investigate the binding behavior of these conjugates on graphene surfaces and assess their potential for creating patterned elastomeric materials.

Main Methods:

• Synthesis of P1/RLP conjugates.
• Quartz crystal microbalance analysis and atomic force microscopy to study graphene binding.
• Molecular simulations to analyze binding modes.

Main Results:

• Parent RLPs showed minimal graphene binding, while P1/RLP conjugates formed dense, patterned bioligand overlayers.
• Molecular simulations revealed a diffuse binding mode for P1/RLP conjugates, involving more residues with moderate contact, unlike typical anchor-residue binding.
• Analysis indicated that RLP2-based conjugates on graphene offer increased availability of Tyr residues for cross-linking.

Conclusions:

• P1/RLP conjugates facilitate controlled organization on graphene surfaces, overcoming limitations of natural resilin.
• The diffuse binding mode and enhanced Tyr residue availability provide a framework for developing novel, patterned elastomeric biomaterials with tunable properties.