Study of the Chemical Synthesis of Peptides

In recent decades, umpteen peptide hormones have been formulated. Some of these include insulin, human growth hormone, and luteinizing hormone releasing hormone. In addition, recombinant methods have been used to realise create from raw stuff plasminogen activator and human erythropoietin.

The chemical substance syntheses of peptides generally involves the incorporation of amino blistery residues into growing polypeptide chains. This whitethorn involve the following chemical move: (1) protection; (2) coupling; (3) deprotection; (4) isolation; and (5) characterization of the intermediates. With large peptides unruffled of many amino acids, these steps female genitalia be some(prenominal) repetitive and time-consuming. Fortunately, various processes have been developed to make the procedures slight difficult (2:249-263).

Most chemical syntheses employ either straightforward phase peptide subtraction (SPPS) or liquid phase peptide subtraction (LPPS) methods (5:3697). Solid phase peptide synthesis techniques were developed by Merrifield (1963). The investigator used SPPS to synthesize tetrapeptide L-leucyl-L-alanyl-glycyl-L-valine (1:147). The methods typically involve attaching amino acids to an water-insoluble polymeric put forward. Such supports may consist of resins or gels. Peptide derivatives carry on attached to the support during washing. They are solely separated from the support when chain building is complete (1:147).

Solid phase peptide synthesis, therefore, provides an leisurely way of separating peptide d

Perhaps the almost successful coupling reagent was introduced by Sheehan & Hess (1955). The introduction of dicyclohexylcarbodiimide represented a significant milestone in the history of peptide synthesis. The reagent can hardly be added to mixtures containing both carboxyl and amine components. Through intramolecular rearrangements, the reagent permits "activation and coupling to proceed concurrently (1:14-16, 55-70)."

3. Bongers, J.; Heimer, E. P. Recent applications of enzymatic peptide synthesis. Peptides. 15:183-193; 1994, January.

Third, side reactions can involve over reaction. For example, overactivated carboxyl-component derivatives may be too reactive to be selective.

Thus, they may acylate not only the desired amino group, but other nucleophiles as well. Both the symmetrical and mixed anhydrides are examples of overactivated derivatives (2:169-214).

The chemical synthesis of peptides obviously has a very long history. At the opening of the 20th century, scientists were formulating simple peptide derivatives. They are currently able to create complex, physiologically-active polypeptides. Considering that recombinant methods remain in a nascent stage of development, it seems only reasonable to conclude that the future holds further advances in the chemical synthesis of peptides.

In the future, more and more peptides may be synthesized using recombinant techniques. One of the first successful applications of the methods involved the facial expression of a synthetic somatostatin gene as a alignment protein in Escherichia coli (9:4599). However, many problems need to be solved, before recombinant proteins can be produced on an industrial scale (8:23-33).

Peptide synthesis typically occurs at or below room temperature. However, since amide bond make-up requires energy, one of the species involved in the reaction must be activated. Various researchers have considered activating the amino group. For example, the reactivity of the (
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