Air Force

Protein functionalized carbon nanotubes as a biosensor

Stable and multifunctional peptide sequences non-covalently bind to the surface of single-walled carbon nanotubes (SWNTs), recognize target molecules such as chemicals, biological materials and toxins, and trigger an electronic signal

Medical & Biotechnology

Peptide P1ASP1C structure prediction using molecular dynamics simulations. Starting three different initial conformations A, B, and C (left panels) and equilibrated structures (right panels). An interaction between Trp17-Phe18 from one side and Tyr4 -Trp6 -Tyr5 from the other side stabilizes the sheet structure, while the bulkiness of Asn9 – Asn10-Lys11-Thr12 destabilizes the helix structure.

Nanotube-based sensors functionalized with naturally occurring biomolecules, such as enzymes and antibodies/antigens, often require an auxiliary mechanical or chemical linking mechanism to attach the functionalizing agent to the nanotube. The biomolecule alone is usually unable to bind to both the SWNT and the target molecule. In addition, many biomolecules are susceptible to loss of biological activity upon binding to a substrate such as a carbon nanotube and also to instability and degradation upon environmental exposure.

As an answer to the above problems, Air Force researchers have developed an improved biosensor leveraging the benefits of SWNTs in sensing conductivity changes together with peptide sequences designed to specifically recognize and bind to target molecules. Binding to targets of interest creates a conductivity change in the SWNT which can be electronically detected. These peptides bind directly to the SWNTs and to the target.

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