Taking a Look at How Peptides are Produced Chemically

Taking a Look at How Peptides are Produced Chemically
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After the invention of solid-phase synthetic procedures in 1963, the research groups that work on peptide synthesis increased greatly.

But the actual method of producing peptides chemically has its own set of limitations. When the Fmoc and Boc protecting groups were developed, new methods, such as the novel amino acid groups, came to light.

These methods helped in producing high quantity and quality peptide-related productions. In the 1980s, researchers used the “fragment condensation” method to create peptides chemically.

But the rate of reaction and racemization proved the method to be not ideal for peptide production.

Things to Know About Peptide Synthetic Methods

There are different types of peptide synthesis techniques, and each of them is based on chemical procedures. These chemical procedures carry over 100 years of history.

In 1881, Theodore Curtis became the first to synthesize the N-protected dipeptide, known as “Benzoylglycylglycine.” Here, Curtis utilized the “azide-coupling” technique, where the glycerin’s silver salt got treated with “Benzoylchloride.”

But the first-ever synthetic dipeptide published was called “Glycylglycin” and was synthesized by Emil Fischer back in 1901. Fischer synthesized the peptide through “hydrolysis” of “glycine diketopiperazine.”

Fischer’s peptide synthesis was marked as the start of peptide chemistry. But when it comes to peptide synthesis, there are countless synthetic difficulties. To overcome these difficulties, amino-protecting groups were needed.

So, in 1931, Zerwas and Bergmann created the “carbobenzoxy group. Along with that, Albertson, McKay, and Carpino introduced the Tert-Butyloxycarbonyl group back in 1957.

But it was the American Biochemist Robert Bruce Merrifield who discovered SPPS or “Solid Phase Peptide Synthesis” back in 1963. Here, Merrifield used the “solid support” technique to synthesize the peptide sequences.

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The Methods of Peptides Synthesis

At present, there are two methods available to produce peptides chemically. These two methods are Solid Phase Peptide Synthesis [SPPS] and Solution Phase Synthesis [SPS]. Let’s learn about these two methods in detail. You can also check Lotilabs to buy high-quality peptides.

The Solution Phase Synthesis [SPS]

The SPS technique is the grouping of all the single amino acids in one solution. For synthesizing the long peptides, experts used the “fragment condensation technique.”

Here, all the small fragments of the needed peptide get synthesized first and then grouped together to create the long peptide. The benefit of this technique is that the intermediate products will be purified and deprotected.

This will lead to the final peptide being of high purity. Some of the examples of the peptides which were synthesized by this technique are oxytocin, human insulin, and porcine gastrin-releasing peptide.

The Solid Phase Peptide Synthesis [SPPS]

Under the SPPS technique, experts utilize the resin as support. The alpha amino acids and amino acids paired with provisional protecting groups get attached to the resin through the C-terminus.

After that, the protecting groups are removed, and the resin is washed before any subsequent additions. This technique gets repeated until the entire sequence is finished.

Ending Note

Synthetic peptides are produced chemically through the SPPS or SPS methods. These chemically-made peptides are used in research by experts in laboratories. But remember, these peptides are not designed for human consumption and are used only for medical studies.

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