Chemists recover mixed folded proteins to life


Scientists from ITMO University in Saint Petersburg and Hebrew University in Jerusalem have found a way to recover a protein structure after its chemical denaturation make folded proteins. Denaturation is a process in which proteins or nucleic acids lose the quaternary structure, tertiary structure and secondary structure which is present in their native state. By application of some external stress or compound such as a strong acid or base.

The method electrostatic interaction used between folded, or denatured, proteins and alumina, to unwrap them. Method works for both specific molecules and multi protein systems. No previous technique has been able to recover mixtures of enzymes before. This can simplify and cheapen the production of drug proteins for Alzheimer’s and Parkinson’s treatment. Proteins, especially accelerators of chemical reactions, are the basis of the pharmaceutical and food industries.

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Protein Folding technique

Protein folding is the process by which a protein structure assumes its functional shape or conformation. All protein molecules heterogeneous unbranched chains of amino acids. By coiling and folding into a specific three-dimensional shape they are able to perform their biological function.

Meanwhile, 80 percent of these substances are lost during synthesis. Influenced by unfavorable factors like strong acids, alkali or heating, proteins denature, losing their native shape and any chemical activity. Thus, the industry seeks a universal method for recovering protein structure, which could make the production cheaper and more effective.

To manufacture enzyme-based drugs and foods on an industrial scale, it is especially important to find a way to recover mixtures of proteins, since renaturating each particular type of enzyme separately is costly and inefficient.

Unfolded molecules of Enzymes

Chemists have proposed a solution to this issue with a process that gives a second life to proteins, returning their molecules to the original form after denaturation. The chemist’s unfolded molecules of three enzymes: carbonic anhydrase, phosphatase and peroxidase. Denatured by strong alkaline, the proteins mixed with nanoparticles of alumina in water. Due to electrostatic interaction, the enzymes attracted the nanoparticles and engaged them in forming a supramolecular complex with physical rather than chemical bonds.

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This shell of nanoparticles protected protein molecules from aggregation, enabling the scientists to easily extract them from the aggressive media. Washed from denaturing substances, the enzymes restored their structure by themselves.

Constant exposure of denaturing agents and the tendency of curling macromolecules to aggregation are major obstacles for recovering proteins. When removing these factors, we were able to regenerate our objects. Changing pH, the scientists separated nanoparticles from proteins showing that the substances involved in the experiment can be repeatedly used.