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Better way to purify peptide-based drugs by adding atoms to the mix

Date:
February 18, 2014
Source:
Michigan Technological University
Summary:
During the production of peptide drugs, amino acids attach to each other in chains, but some of the chains are never completed. To separate these truncated peptides from the good ones, a team of researchers adds a polymerizable group of atoms to the mix. These atoms bind to either the perfect peptides or the unfinished ones, but not to both. The polymerized peptides become insoluble and precipitate out of the solution.

Members of Shiyue Fang's research team in his lab at Michigan Tech, where they developed a better process to purify peptides and other biomolecules.
Credit: Image courtesy of Michigan Technological University

Peptides are an intriguing class of drugs. They are made of amino acids, just as humans are, and because of their intimate relationship with our own biological molecules, they have the potential to fight some of the most intractable diseases, including cancer.

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But they can be difficult and expensive to make. A year's worth of the anti-HIV peptide drug enfuvirtide costs $25,000. Now a chemist at Michigan Technological University has overcome an important hurdle in the manufacturing process by developing a quicker, simpler purification method. As a bonus, his technique also works on DNA.

The new technology separates perfect peptides from those that do not make the grade, says Shiyue Fang. During production, amino acids attach to each other in chains to form the desired peptide, but some of the chains are never completed. To separate these truncated peptides, Fang's team adds a polymerizable group of atoms to the mix.

These atoms bind to either the perfect peptides or the unfinished ones, but not to both. The polymerized peptides become insoluble and precipitate out of the solution. "Just take the solution out, and the peptides are separated," said Fang.

The method works in about two hours, much faster than a similar process Fang developed a few years ago. And it works equally well for DNA sequences.

The process has other advantages. It is cheaper and requires less labor than existing peptide purification methods, it can handle large batches of peptides at a time, and it generates less waste. "Other methods use a large amount of organic solvents, with a waste-to-product ratio of about 1,000:1. Our waste-to-product ratio is 50:1, maximum," said Fang. "And it takes less time."

Fang has been issued a patent for his discovery and is exploring its commercial potential. "I'm excited about the progress we've made," he said. "Peptide drugs are used to fight cancer, inflammation, diseases of the central nervous system, viral diseases like HIV. . . This gives us a chance to make a difference in people's lives."

An article on the research, "Purification of Synthetic Peptides Using a Catching Full-Length Sequence by Polymerization Approach," coauthored by Fang, postdoctoral fellow Mingcui Zhang and graduate student Durga Pokharel, was published online in the journal Organic Letters.


Story Source:

The above story is based on materials provided by Michigan Technological University. The original article was written by Marcia Goodrich. Note: Materials may be edited for content and length.


Journal Reference:

  1. Mingcui Zhang, Durga Pokharel, Shiyue Fang. Purification of Synthetic Peptides Using a Catching Full-Length Sequence by Polymerization Approach. Organic Letters, 2014; 140214115100000 DOI: 10.1021/ol403426u

Cite This Page:

Michigan Technological University. "Better way to purify peptide-based drugs by adding atoms to the mix." ScienceDaily. ScienceDaily, 18 February 2014. <www.sciencedaily.com/releases/2014/02/140218114233.htm>.
Michigan Technological University. (2014, February 18). Better way to purify peptide-based drugs by adding atoms to the mix. ScienceDaily. Retrieved December 19, 2014 from www.sciencedaily.com/releases/2014/02/140218114233.htm
Michigan Technological University. "Better way to purify peptide-based drugs by adding atoms to the mix." ScienceDaily. www.sciencedaily.com/releases/2014/02/140218114233.htm (accessed December 19, 2014).

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