Abstract
Peptide drug development has made great progress in the last decade thanks to new production, modification, and analytic technologies. Peptides have been produced and modified using both chemical and biological methods, together with novel design and delivery strategies, which have helped to overcome the inherent drawbacks of peptides and have allowed the continued advancement of this field. A wide variety of natural and modified peptides have been obtained and studied, covering multiple therapeutic areas. This review summarizes the efforts and achievements in peptide drug discovery, production, and modification, and their current applications. We also discuss the value and challenges associated with future developments in therapeutic peptides.
Highlights
Therapeutic peptides are a unique class of pharmaceutical agents composed of a series of well-ordered amino acids, usually with molecular weights of 500-5000 Da1
Research into therapeutic peptides started with fundamental studies of natural human hormones, including insulin, oxytocin, vasopressin, and gonadotropin-releasing hormone (GnRH), and their specific physiological activities in the human body[2]
We focus on the pharmaceutical characteristics of therapeutic peptides and highlight new technologies that have improved the design, synthesis, modification, and evaluation of peptide drugs, and provide new perspectives in the applications of peptide drugs
Summary
Therapeutic peptides are a unique class of pharmaceutical agents composed of a series of well-ordered amino acids, usually with molecular weights of 500-5000 Da1. Stapled peptides represent a recent new cross- translational machinery, leading to the production of structurally linking approach introduced to stabilize the α-helix structure, and functionally diverse peptides, and allowing these molecules to using non-natural electrophilic amino acids to replace residues at overcome the inherent limitations of common peptide drugs. The modification of peptides to stabilize growth hormone are representative examples of the many β-sheets is usually achieved by the introduction of D-amino acids, available peptide drugs made using recombinant DNA technolsuch as D-Pro, to form a turn structure in the sequence. Li et al.[267] recently reported on a proximity-enabled reactive therapeutics (PERx) strategy to develop covalent protein drugs They genetically incorporated the latent bioactive ncAA, fluorosulfate-L-tyrosine (FSY)[268], into human programmed cell death protein 1 (PD-1) at position 129 and showed that the resulting PD-1(FSY) formed covalent bonds selectively with its natural ligand, PD-L1, in vitro and in vivo. No peptide vaccines have yet been approved for the treatment of COVID-19, valuable experience has been gained in the development of peptide vaccines, against SARS-CoV2, and against new viruses in the future
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