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How Protein Nanotubes Were Made—and Whether the Proteins Still Worked

Researchers built protein nanotubes layer by layer inside porous alumina templates and reported activity in two proteins after fabrication.

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In a 2005 report, researchers led by Charles Martin at the University of Florida made nanotube walls from proteins by building alternating layers inside the pores of an alumina membrane. They reported that glucose oxidase still catalysed glucose oxidation and haemoglobin retained electrochemical activity after fabrication. The work demonstrated a laboratory fabrication method, not a finished medical or commercial technology.

How did the researchers make protein nanotubes?

The team used a porous alumina membrane as a temporary mould. According to Chemistry World’s 2005 account, the membrane was 60 µm thick and contained billions of pores, each 200 nm in diameter.

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  1. Prepare the pore walls. The researchers attached a monolayer of 3-aminopropylphosphonic acid to the inside of the alumina pores.
  2. Build the protein walls. They alternated glutaraldehyde, a protein immobilisation agent, with the selected protein. Repeating these layers inside the pores formed the nanotube walls. The proteins were structural building material, not simply cargo attached to a pre-existing tube.
  3. Release the tubes. After deposition, the membrane was immersed in phosphoric acid to remove the alumina template and release the nanotubes.

How did layer count affect wall thickness?

The reported 2005 experiment linked the number of deposited protein layers to wall thickness:

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Protein layers Reported wall thickness
Three 15 nm
Six 30 nm

These are experimental dimensions from the reported fabrication, not a general guarantee for other proteins or procedures.

Did the proteins remain functional?

The account names two proteins and reports a different activity for each. Glucose oxidase nanotubes catalysed glucose oxidation, while haemoglobin nanotubes retained haem electroactivity. The researchers treated those results as evidence that the proteins had not been denatured during fabrication.

The reported tests support the narrower conclusion that these activities were observed in the tested nanotubes. They do not establish that every protein would retain its function, or that the method would behave identically in other laboratories.

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What might protein nanotubes be used for?

The report identified biosensors and enzymatic bioreactions as possible uses. Martin’s team was also interested in drug delivery and bio-imaging, but these were prospective applications, not demonstrated clinical or commercial uses. Martin described 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, clinical effectiveness, or practical performance in people. Its findings concern a laboratory fabrication approach and activity measurements for two proteins.

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