Journals on Medical Genetics - BJSTR Journal

Abstract

Peptides can be defined as #polypeptide chains of 50 or less amino acids or 5000 Da in molecular weight characterized by a high degree of secondary structure and lack of tertiary structure. Therapeutic peptides have traditionally been derived from nature as naturally occurring peptide hormones (known as bioactive peptides), genetic/recombinant libraries and chemical libraries [1]. The recent technologies used for peptides production include chemical synthesis, #enzymatic synthesis, recombinant DNA #biotechnology, cell-free expression and transgenic animal or plant species. The possibility to determine the most suitable one for each peptide production depends on peptide size. The use of unnatural amino acids and #pseudo-peptide bonds make chemical synthesis offering wider chemical diversity than other peptide derivatives produced by recombinant DNA technologies or bio-catalysis. The advantage of Large-scale production of chemical synthesis makes it a viable technology especially for the production of small and medium-sized peptides ranging from approximately 5 to 50 residues [2]. Over the years, peptides have been evolved as promising #therapeutic agents in the treatment of different disease as cancer, diabetes, and cardiovascular diseases. Therapeutic application of peptides for other treatments is growing rapidly [3].

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Peptides as Drug Candidates: Limitations and Recent Development Perspectives by Yusuf A. Haggag in BJSTR