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21 Carboxylic Acid Derivatives -- Part 19
Total synthesis of peptides is not an economical method for commercial production.
The important peptides are usually derived from biological sources.
It was taken from the pig pancreas.
The quality and availability of peptide pharmaceuticals have improved.
Amino Acids, Peptides, andProteins are inserted into a bacterium to cause it to produce aProtein.
An important area of chemistry is laboratory peptide synthesis.
If the synthetic peptide turns out to be the same as the natural one, it proves that the structure is correct.
The synthesis provides more products.
Synthetic peptides can be made with altered amino acid sequence to compare their biological activity with natural peptides.
The critical areas of goat's milk can be pointed out by these comparisons.
Hemophiliac factor may suggest causes and treatments for genetic diseases with similar VIII and tissue abnormal peptides.
Peptide synthesis requires the formation of amide bonds between the proper amino dissolving clot.
We would form an amide with simple acids and amines by converting the acid to an activated derivative.
Adding amine and vaccines for diseases.
Genetically modified yeasts and tobacco.
There is a carboxyl group and an amino group in each of the acids.
The carboxyl group reacts with its own group.
Every conceivable sequence can be formed if we mix some amino acids and add a reagent.
There are side chains that might interfere with peptide formation.
There is an extra carboxyl group and an extra amino group inglutamic acid and lysine.
As a result, peptide synthesis always involves the formation of desired bonds and the blocking of unwanted bonds.
Chemists have developed many techniques.
They used typical solution techniques before 1963.
The chemists would apply protecting groups, add activated groups, and then purify the product.
Robert Bruce Merrifield of Rockefeller University developed a method for making peptides without having to purify the intermediates.
He attached the growing chains to the beads.
The excess reagents are washed away by rinsing the beads.
Merrifield was able to synthesise ribonuclease in 6 weeks using this machine.
Merrifield won the chemistry prize in 1984.
The way we usually draw peptides is to start from the C end and work toward the N end, which is the opposite of Merrifield's method.
The protected C-terminal amino acid is attached to the bead.
The NH2 group must be protected.
After the protecting group is removed, the next protected acid is coupled to the first.
Until the entire peptide is formed, there are many more deprotection andcoupling reactions.
It is cleaved from the bead.
Attach the protected C-terminal amino acid to the bead.
Then de protect the next protected amino acid.
The finished peptide can be cleaved from the bead.
We will only consider one set of reagents for each step.
Regardless of the specific reagents, the general principles are the same.
Solid-phase peptide synthesis requires three reactions.
These reactions attach the first protected amino acid to the solid support and form the bonds between the amino acids.
The synthesis is done in the reverse direction.
It begins at the C end and ends at the N end.
Some of the aromatic rings have chloromethyl groups, which is found in a special polystyrene bead.
The chloromethyl groups are similar to other benzyl halides.
The carboxyl group of an N-protected amino acid is what gives the polymer it's ester.
The alcohol part of an ester protecting group for the carboxyl end of the C-terminal amino acid is served by the polymer.
If the chloromethyl groups are attacked, the amino group must be protected.
The chain is built after the C-terminal amino acid is fixed.
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