NIST studies nanoparticle and protein interaction

13 January 2010

Gold nanoparticles have been found in a number of applications including the diagnosis and treatment of number of human diseases including cancer, however their interaction with human blood proteins have been studied first time. Scientists at NIST (National Institute of Standards and Technology) have now studied and quantified the interaction of gold nanoparticles with human blood proteins. The new finding will help in developing the next generation therapies that could be used for diagnosis and treatments of a number of diseases including cancer.

One of the major advantages of gold nanoparticles is that, these can be functionalized easily if the nanometer size is between 5 and 100 nanometer. Scientists have predicted that the functionalized nanoparticles will interact with protein and this interaction will alter the biochemical activity of protein. The altered protein will behave differently and may have some adverse affect. Researchers led by Douglas at NIST studied the gold nanoparticles with five types of blood proteins with the help of microscope and spectroscopy devices.

Researchers studied the optical properties and found that once the protein stick to a nanoparticle, it changes the optical properties of both. Studying these changes carefully, researchers were able to quantify the stickiness and thickness of absorbed protein on nanoparticles. Researchers found that all five types of protein selected for the study interact with the nanoparticles and once they stick to the nanoparticles, the diameter of the nanoparticles increases, which also increases the stickiness. Researchers are planning to carry out more experimental work to understand how the different sized nanoparticles attached to the human cells.

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One Response to “NIST studies nanoparticle and protein interaction”

  1. On January 22nd, 2010 at 9:43 pm, Elaine Says:

    Can you list the reference details or the journal this study was published in? I’d like to read more about it.

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