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2. A Simple Introduction of Peptide Synthesis Mechanism
3. Peptides - From Discovery to Therapeutics
Peptides are short polyers formed from the peptide bond linking, in a defined order, of α-amino acids. The major classes of peptides include ribosomal peptides, non-ribosomal peptides, peptones
and peptide fragments. The hypothalamic peptide hormone gonadotropin-releasing hormone (GnRH) is an example of ribosomal peptides. The peptide is synthesized by translation of mRNA. GnRH is subjected to a regulatory proteolytic pathway to generate the mature form. Non-ribosomal peptides are usually produced by bacteria or fungi. Nonribosomal peptides often have a cyclic and/or branched structures. For example, Bacitracin is a mixture of related cyclic polypeptides produced by organisms of the licheniformis group. Peptones are derived proteins, which may be produced by hydrolysis of a native protein with an acid or enzyme. Peptide fragments refer to fragments of proteins that are used to identify or quantify the source protein.
Peptides play an important role in molecular biology, biochemistry, immunology and medicine. Synthetic peptides have been widely used for structure-function studies of polypeptides. The processes involve initiation or inhibition through protein-protein interaction. Take a non-formyl peptide (HP-20) for example. The rapid intracellular calcium mobilization of HP-20 was measured for human neutrophils in order to explore its interaction with the formyl peptide receptor (FPR).
The following are the major applications of peptides:
- Cosmetic peptides
- Protein structure and function: immune monitoring, epitope discovery
- Food and healthcare applications: antimicrobial peptides
- Therapeutic peptides

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