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Researchers at the University of Florida reported a way to build nanotube walls from proteins inside porous alumina membranes. They alternated layers of glutaraldehyde and protein, then dissolved the template to release the tubes. Tests reported in 2005 found that glucose oxidase still catalysed glucose oxidation and haemoglobin retained electrochemical activity—evidence that the proteins remained functional through fabrication.
How were the protein nanotubes made?
The method used the pores of a porous alumina membrane as molds. In the 2005 account, the membrane was 60 µm thick and contained billions of pores, each 200 nm in diameter. The researchers first attached a monolayer of 3-aminopropylphosphonic acid to the pore walls, then built up the nanotube walls by alternating glutaraldehyde, a protein-immobilisation agent, with a selected protein. After deposition, they immersed the membrane in phosphoric acid to release the nanotubes. Chemistry World’s 2005 report describes the process and dimensions.
This means the proteins formed the nanotube walls; they were not simply attached to a separate, pre-existing nanotube.
How did layer count affect wall thickness?
The reported wall thickness increased with the number of protein layers:
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| Protein layers | Reported wall thickness |
|---|---|
| Three | 15 nm |
| Six | 30 nm |
These are experimental dimensions reported for the work, not general specifications for protein nanotubes.
Did the proteins remain functional?
The researchers tested two proteins and reported activity after fabrication:
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- Glucose oxidase: the nanotubes catalysed glucose oxidation, demonstrating retained enzymatic activity.
- Haemoglobin: the nanotubes retained haem electroactivity, showing an electrochemical response.
The observations were presented as evidence that the proteins had not been denatured during the process. They establish activity for the proteins and tests reported, not for every protein or every possible use.
What uses did the researchers envision?
The report identified biosensors and enzymatic bioreactions as possible applications. The team was also interested in drug delivery and bio-imaging, but those were prospects, not demonstrated clinical or commercial uses. Team leader Charles Martin characterized the work as early-stage: “This work is in its infancy, but we are very excited about the prospects.” Chemistry World, 2005.
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The account does not establish safety, reproducibility across laboratories, or clinical application. It is a report of an experimental fabrication approach, not evidence that protein nanotubes are available as products or treatments.
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