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Stable And More Durable Fluorinated Proteins Developed

Shreyas

Shreyas

 Updated: 05 Jul 2011

Proteins that are comparable with Teflon polymer in terms of stability and durability have been created. Recently, scientists at New York University Polytechnic have devised a process that makes fluorinated proteins more stable and durable even at extreme limits. NYU-Poly Assistant Professor of Chemical and Biological Sciences Jin Montclare and Peter Baker have successfully demonstrated the modification of existing fluorinated proteins with the help of bacteria. This resulted into the formation of proteins that could sustain temperatures up to 140 degrees Fahrenheit.

The researchers have followed the footprints of their senior, NYU-Poly alumni John Gilbert. The efforts taken by him to evaluate Teflon about 50 years ago, a newly developed polymer then, led to its successful application of fluorinated polymer as a coating for the utensils. Montclare and Baker plan to take the same route in creating better proteins by delving more on fluorinated proteins. The findings were announced in the current issue of ChemBioChem. The proteins developed by them are less susceptible to denaturation than the existing proteins. When the proteins undergo denaturation, their structure is lost due to some external stress, compounds, or heat. The simplest example is the change in the structure of egg while heating it to make an omelet.

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Teflon-like globular proteins

The denaturation of proteins lead to the reduction in reliability in use of the same and scientists are trying very hard to figure out some way or the other so that the proteins do not lose their structural properties at  high temperatures. The researchers at NYU-poly have made a breakthrough by forming these durable fluorinated proteins. These proteins do not lose their structural and functional properties even when the temperatures are high. Such high temperatures would otherwise cause complete breakdown of other proteins. The interfaces of the proteins were reinforced due to which they became more resistant to degradation. The stability was achieved by incorporation of <em>p</em>-fluorophenylalanine (pFF) in the S phosphotriesterase dimer. It was found that the protein became stable and could achieve refoldibitly along with improved operation for substrate at high temperatures.

The problem is that proteins are meant to function for a specific task in a specific environment. In order to get a stable protein, the functional and structural properties were to be retained. In other words, the protein should be “active” in a wide range of environmental conditions.

The fluorinated proteins or Teflon-like proteins can be formed from a wide range of proteins. These proteins are widely used in medicines, especially in cancer drugs. The stable proteins in future can take the role of prophylactics in fighting against exposure to neurotoxic agents. This means a lot to the defense firms as application of these drugs will help a soldier to resist certain neurotoxins to a large extent. For now, scientists are striving for improving the durability of the proteins. As of now, there exist certain difficulties in storing the fluorinated proteins in stable, precise and cheaper way.

Source: Physorg.com
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